Staff information

Biography

Dr. Garry W. Buchko is a physical biochemist that first joined PNNL as a postdoctoral fellow with Dr. Michael Kennedy in 1995 and was promoted to senior scientist in 2001. In 2017 he accepted a joint-appointment as an Associate Professor with the School of Molecular Biosciences at Washington State University. He received his M.Sc. in Chemistry at McMaster University (1986) under the supervision of Drs. Russell Bell and the late Tom Nelson, pioneers in the field of ribonucleic acid synthetic chemistry. This was followed by a doctorate degree in Chemistry at the University of Manitoba (1989) with Dr. Frank Hruska, a pioneer in using NMR spectroscopy to study nucleic acid sugar conformations. His first two postdoctoral experiences were with the radiation biologists Drs. Jean Cadet in Grenoble, France (Laboratoire des Lesions des Acides Nucléique, Centre d'Etudes Nucléaires de Grenoble) and Michael Weinfeld in Edmonton, Alberta (Cross Cancer Institute). His third postdoctoral experience was with the NMR spectroscopist/protein biochemist Dr. Bob Cushley in Burnaby, British Columbia (Institute of Molecular Biology and Biochemistry, Simon Fraser University). Currently, Dr. Buchko is the PNNL-WSU component of the Seattle Structural Genomics Center for Infectious Disease (SSGCID, www.ssgcid.org), a consortium of researchers at the Center for Infectious Disease Research (formerly Seattle BioMed), Beryllium (formerly Emerald BioStructures), and the University of Washington. SSGCID is funded by the National Institute of Allergies and Infectious Diseases (NIAID) and devoted to applying state-of-the-art structural genomics technologies to structurally characterize targeted proteins from NIAID Category A-C pathogens and organisms. In addition to the SSGCID structural biology efforts, Dr. Buchko is also part of a team of PNNL scientists, lead by Dr. Wendy Shaw and funded by National Institute of Dental and Craniofacial Research, studying amelogenin's role in the formation of tooth enamel (biomineralization).

Research Interests

• Structural biology (protein structures solved by NMR-based methods or X-ray crystallography).
• Protein function analysis. A common approach is to determine a structure by XRD and then identify protein-ligand interactions in solution using a suite of NMR experiments (eg: chemical shift perturbation).
• Biophysical characterization of proteins using a suite of spectroscopies.
• Protein thermodynamics (isothermal titration calorimetry).
• Protein dynamics.
• Intrinsically disordered proteins.
• Protein-DNA interactions.
• Infectious diseases.
• Biomineralization.

Education and Credentials

• Ph.D., Chemistry, University of Manitoba (1989)
• M.Sc., Chemistry, McMaster University (1986)
• B.Sc.(Hons), Biochemistry, University of Manitoba (1983)

Affiliations and Professional Service

• Associate Professor - School of Molecular Biosciences, Washington State University.

PNNL Publications

2023

• Buchko G.W., M. Zhou, C.H. Vesely, J. Tao, W.J. Shaw, R.A. Mehl, and R.B. Cooley. 2023. "High-yield recombinant bacterial expression of 13C-, 15N-labelled, serine-16 phosphorylated, murine amelogenin using a modified third generation genetic code expansion protocol." Protein Science 32, no. 2:Art. No. e4560. PNNL-SA-179449. doi:10.1002/pro.4560
• Taylor S.D., J. Tao, Y. Shin, G.W. Buchko, A. Dohnalkova, J.R. Grimm, and B.J. Tarasevich, et al. 2023. "Resolving protein-mineral interfacial interactions during in vitro mineralization by atom probe tomography." Materials Today Advances 18. PNNL-SA-174054. doi:10.1016/j.mtadv.2023.100378

2022

• Buchko G.W., S.T. Mergelsberg, B.J. Tarasevich, and W.J. Shaw. 2022. "Residue-specific insights into the intermolecular protein-protein interfaces driving amelogenin self-assembly in solution." Biochemistry 61, no. 24:2909-2921. PNNL-SA-177235. doi:10.1021/acs.biochem.2c00522
• Laureanti J.A., G.W. Buchko, M.T. Oostrom, B. Ginovska, and W.J. Shaw. 2022. Understanding Proton Movement in [Fe-Fe] Hydrogenases. PNNL-33326. Richland, WA: Pacific Northwest National Laboratory. Understanding Proton Movement in [Fe-Fe] Hydrogenases
• Mandel C., H. Yang, G.W. Buchko, J. Abendroth, N. Grieshaber, T. Chiarelli, and S. Grieshaber, et al. 2022. "Expression and structure of the Chlamydia trachomatis DksA ortholog." Pathogens and Disease 80, no. 1:Art. No. ftac007. PNNL-SA-149650. doi:10.1093/femspd/ftac007
• Tao J., E. Hanson, A. Dohnalkova, G.W. Buchko, B. Jin, W.J. Shaw, and B.J. Tarasevich. 2022. "Changes in the C-terminal, N-terminal, and Histidine Regions of Amelogenin Reveal the Role of Oligomer Quaternary Structure on Adsorption and Hydroxyapatite Mineralization." Frontiers in Physiology 13. PNNL-SA-159591. doi:10.3389/fphys.2022.1034662
• Wu R., C. Smith, G.W. Buchko, I.K. Blaby, A. Paez-Espino, N.C. Kyrpides, and Y. Yoshikuni, et al. 2022. "Structural characterization of a soil viral auxiliary metabolic gene product - a functional chitosanase." Nature Communications 13, no. 1:Art. No. 5485. PNNL-SA-170607. doi:10.1038/s41467-022-32993-8

2021

• Choi R., M. Zhou, R. Shek, J.W. Wilson, L. Tillery, J.C. Craig, and I.A. Salukhe, et al. 2021. "High-throughput screening of the ReFRAME, Pandemic Box, and COVID Box drug repurposing libraries against SARS-CoV-2 nsp15 endoribonuclease to identify small-molecule inhibitors of viral activity." PLoS One 16, no. 4:e0250019. PNNL-SA-159108. doi:10.1371/journal.pone.0250019

2020

• Buchko G.W., J. Abendroth, J.I. Robinson, I. Phan, P.J. Myler, and T.E. Edwards. 2020. "Structural diversity in the mycobacteria DUF3349 superfamily." Protein Science 29, no. 3:670-685. PNNL-SA-147115. doi:10.1002/pro.3758
• Elnaas A.R., D. Grice, J. Han, Y. Feng, A. Di Capau, T. Mak, and J.A. Laureanti, et al. 2020. "Discovery of a Natural Product that Binds to the Mycobacterium tuberculosis Protein Rv1466 by Native Mass Spectrometry." Molecules 25, no. 10:2384. PNNL-SA-152797. doi:10.3390/molecules25102384
• Laureanti J.A., B. Ginovska, G.W. Buchko, G.K. Schenter, M.A. Hebert, O. Zadvornyy, and J. Peters, et al. 2020. "A Positive Charge in the Outer Coordination Sphere of an Artificial Enzyme Increases CO2 Hydrogenation." Organometallics 39, no. 9:1532-1544. PNNL-SA-149994. doi:10.1021/acs.organomet.9b00843
• Ma Z., J. Abendroth, G.W. Buchko, K.H. Rohde, and V.L. Davidson. 2020. "Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis." Biochemical Journal 477, no. 2:567-581. PNNL-SA-147766. doi:10.1042/BCJ20190827
• Shaheen S., K.F. Barrett, S. Subramanian, S.L. Arnold, J.A. Laureanti, P.J. Myler, and W.C. Van Voorhis, et al. 2020. "Solution structure for an Encephalitozoon cuniculi adrenodoxin-like protein in the oxidized state." Protein Science 29, no. 3:809-817. PNNL-SA-150252. doi:10.1002/pro.3818
• Shaw W.J., B.J. Tarasevich, G.W. Buchko, R.M. Jayasinha Arachchige, and S.D. Burton. 2020. "Controls of Nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite." Journal of Structural Biology 212, no. 3:Article No. 107630. PNNL-SA-153314. doi:10.1016/j.jsb.2020.107630
• Velivelli S.L., K. Czymmack, H. Li, J.B. Shaw, G.W. Buchko, and D. Shah. 2020. "Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection." Proceedings of the National Academy of Sciences (PNAS) 117, no. 27:16043-16054. PNNL-SA-150641. doi:10.1073/pnas.2003526117
• Xie Y., Y. Feng, A. Di Capua, T. Mak, G.W. Buchko, P.J. Myler, and M. Lui, et al. 2020. "A Phenotarget Approach for Identifying an Alkaloid Interacting with the Tuberculosis Protein Rv1466." Marine Drugs 18, no. 3:149. PNNL-SA-150251. doi:10.3390/md18030149

2019

• Laureanti J.A., G.W. Buchko, S. Katipamula, Q. Su, J.C. Linehan, O. Zadvornyy, and J.W. Peters, et al. 2019. "Protein Scaffold Activates Catalytic CO2 Hydrogenation by a Rhodium Bis(diphosphine) Complex." ACS Catalysis 9, no. 1:620-625. PNNL-SA-135805. doi:10.1021/acscatal.8b02615
• Tao J., Y. Shin, R.M. Jayasinha Arachchige, G.W. Buchko, S.D. Burton, A. Dohnalkova, and Z. Wang, et al. 2019. "The energetic basis for hydroxyapatite mineralization by amelogenin variants provides insights into the origin of amelogenesis imperfecta." Proceedings of the National Academy of Sciences (PNAS) 116, no. 28:13867-13872. PNNL-SA-143391. doi:10.1073/pnas.1815654116

2018

• Buchko G.W., R.M. Jayasinha Arachchige, J. Tao, B.J. Tarasevich, and W.J. Shaw. 2018. "Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amleogenin peptide using a nuclear magnetic resonance spectroscopy based method." Archives of Oral Biology 93. PNNL-SA-132678. doi:10.1016/j.archoralbio.2018.06.001
• Buchko G.W., S.N. Hewitt, S.N. Hewitt, W.C. Van Voorhis, and P.J. Myler. 2018. "Solution NMR Structures of Oxidized and Reduced Ehrlichia chaffeensis thioredoxin: NMR-Invisible Structure Owing to Backbone Dynamics." Acta Crystallographica. Section F 74, no. 1:46-56. PNNL-SA-126464. doi:10.1107/S2053230X1701799X
• Buchko G.W., S.V. Pulavarti, V. Ovchinnikov, E.A. Shaw, S.A. Rettie, P.J. Myler, and M. Karplus, et al. 2018. "Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides." Protein Science 27, no. 9:1611-1623. PNNL-SA-129358. doi:10.1002/pro.3453
• Jayasinha Arachchige R.M., S.D. Burton, J. Lu, B. Ginovska, L.K. Harding, M.E. Taylor, and J. Tao, et al. 2018. "Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite." Biophysical Journal 115, no. 9:1666-1672. PNNL-SA-131727. doi:10.1016/j.bpj.2018.08.027
• Mori S., K.D. Green, R. Choi, G.W. Buchko, M.G. Fried, and S. Garneau-Tsodikova. 2018. "Using MbtH-like proteins to alter substrate profile of a nonribosomal peptide adenylation enzyme." Chembiochem 19, no. 20:2186-2194. PNNL-SA-131568. doi:10.1002/cbic.201800240

2017

• Boralugodage N., R.M. Jayasinha Arachchige, A. Dutta, G.W. Buchko, and W.J. Shaw. 2017. "Evaluating the Role of Acidic, Basic, and Polar Amino Acids and Dipeptides on a Molecular Electrocatalyst for H2 Oxidation." Catalysis Science & Technology 7, no. 5:1108-1121. PNNL-SA-122890. doi:10.1039/c6cy02579j
• Buchko G.W., M.C. Clifton, E. Wallace, K.A. Atkins, and P.J. Myler. 2017. "Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus." Biomolecular NMR Assignments 11, no. 1:51-56. PNNL-SA-119309. doi:10.1007/s12104-016-9719-2
• Buchko G.W., N. Echols, E.M. Flynn, H. Ng, S. Stephenson, H. Kim, and P.J. Myler, et al. 2017. "Structural and biophysical characterization of the Mycobacterium tuberculosis protein Rv0577, a protein associated with neutral red staining of virulent tuberculosis strains and homologue of the Streptomyces coelicolor protein KbpA." Biochemistry 56, no. 30:4015-4027. PNNL-SA-125503. doi:10.1021/acs.biochem.7b00511
• Zerfass C., G.W. Buchko, W.J. Shaw, S. Hobe, and H. Paulsen. 2017. "Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P5S3 during silicic acid condensation and silica decondensation." Proteins. Structure, Function, and Bioinformatics 85, no. 11:2111-2126. PNNL-SA-116568. doi:10.1002/prot.25366

2016

• Bhardwaj G., V.K. Mulligan, C.D. Bahl, J.M. Gilmore, P. Harvey, O. Cheneval, and G.W. Buchko, et al. 2016. "Accurate de novo design of hyperstable constrained peptides." Nature 538, no. 7625:329-335. PNNL-SA-117706. doi:10.1038/nature19791
• Buchko G.W., A. Perkins, D. Parsonage, L.B. Poole, and P.A. Karplus. 2016. "Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics." Biomolecular NMR Assignments 10, no. 1:57-61. PNWD-SA-10489. doi:10.1007/s12104-015-9637-8
• Priyadarshani N., A. Dutta, B. Ginovska-Pangovska, G.W. Buchko, M.J. O'Hagan, S. Raugei, and W.J. Shaw. 2016. "Achieving Reversible H2/H+ Interconversion at Room Temperature with Enzyme-Inspired Molecular Complexes: A Mechanistic Study." ACS Catalysis 6, no. 9:6037-6049. PNNL-SA-115312. doi:10.1021/acscatal.6b01433
• Reback M.L., B. Ginovska-Pangovska, G.W. Buchko, A. Dutta, N. Priyadarshani, B.L. Kier, and M.L. Helm, et al. 2016. "Investigating the role of chain and linker length on the catalytic activity of an H2 production catalyst containing a b-hairpin peptide." Journal of Coordination Chemistry 69, no. 11-13:1730-1747. PNNL-SA-116292. doi:10.1080/00958972.2016.1188924

2015

• Baugh L., I. Phan, D.W. Begley, M.C. Clifton, B. Armour, D.M. Dranow, and B.M. Taylor, et al. 2015. "Increasing the Structural Coverage of Tuberculosis Drug Targets." Tuberculosis 95, no. 2:142-148. PNWD-SA-10201. doi:10.1016/j.tube.2014.12.003
• Buchko G.W., and W.J. Shaw. 2015. "Improved protocol to purify untagged amelogenin - Application to murine amelogenin containing the equivalent P70 ? T point mutation observed in human amelogenesis imperfecta." Protein Expression and Purification 105, no. 1:14-22. PNNL-SA-104877. doi:10.1016/j.pep.2014.09.020
• Buchko G.W., J. Abendroth, M.C. Clifton, H. Robinson, Y. Zhang, S.N. Hewitt, and B.L. Staker, et al. 2015. "Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum, the protozoal parasite responsible for cryptosporidiosis." Acta Crystallographica. Section F F71, no. 5:522-530. PNWD-SA-10432. doi:10.1107/S2053230X14028210
• Buchko G.W., T.E. Edwards, S.N. Hewitt, I. Phan, W.C. Van Voorhis, S.I. Miller, and P.J. Myler. 2015. "Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS - "missing" resonances at the dimer interface." Biomolecular NMR Assignments 9, no. 2:381-385. PNWD-SA-10406. doi:10.1007/s12104-015-9614-2
• Staker B.L., G.W. Buchko, and P.J. Myler. 2015. "Recent contributions of structure-based drug design to the development of antibacterial compounds." Current Opinion in Microbiology 27, no. 1:133-138. PNWD-SA-10518. doi:10.1016/j.mib.2015.09.003
• Tao J., G.W. Buchko, W.J. Shaw, J. De Yoreo, and B.J. Tarasevich. 2015. "Sequence-defined Energetic Shifts Control the Disassembly Kinetics and Microstructure of Amelogenin Adsorbed onto Hydroxyapatite (100)." Langmuir 31, no. 38:10451-10460. PNNL-SA-114189. doi:10.1021/acs.langmuir.5b02549
• Tarasevich B.J., J.S. Philo, N.K. Maluf, S. Krueger, G.W. Buchko, G. Lin, and W.J. Shaw. 2015. "The Leucine-Rich Amelogenin Protein (LRAP) is primarily monomeric and unstructured in physiological solution." Journal of Structural Biology 190, no. 1:81-91. PNNL-SA-105350. doi:10.1016/j.jsb.2014.10.007

2014

• Lu J., S.D. Burton, Y. Xu, G.W. Buchko, and W.J. Shaw. 2014. "The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength." Frontiers in Physiology 5. PNNL-SA-102903. doi:10.3389/fphys.2014.00254
• Reback M.L., G.W. Buchko, B.L. Kier, B. Ginovska-Pangovska, Y. Xiong, S. Lense, and J. Hou, et al. 2014. "Enzyme Design From the Bottom Up: An Active Nickel Electrocatalyst with a Structured Peptide Outer Coordination Sphere." Chemistry - A European Journal 20, no. 6:1510-1514. PNNL-SA-96857. doi:10.1002/chem.201303976
• Zhang Y., Y. Zheng, L. Qin, S. Wang, G.W. Buchko, and M.R. Garavito. 2014. "Structural characterization of a ß-hydroxyacid dehydrogenase from Geobacter sulfurreducens and Geobacter metallireducens with succinic semialdehyde reductase activity." Biochimie 104. PNNL-SA-100559. doi:10.1016/j.biochi.2014.05.002

2013

• Baugh L., L.A. Gallagher, R. Patrapuvich, M.C. Clifton, A.S. Gardberg, T.E. Edwards, and B. Armour, et al. 2013. "Combining Functional and Structural Genomics to Sample the Essential Burkholderia Structome." PLoS One 8, no. 1:e53851. PNWD-SA-9931. doi:10.1371/journal.pone.0053851
• Buchko G.W., A. Jain, M.L. Reback, and W.J. Shaw. 2013. "Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-NH2 in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol." Canadian Journal of Chemistry 91, no. 6:406-413. PNNL-SA-90953. doi:10.1139/cjc-2012-0429
• Buchko G.W., G. Lin, B.J. Tarasevich, and W.J. Shaw. 2013. "A solution NMR investigation into the impaired self-assembly properties of two murine amelogenins containing the point mutations T21?I or P41?T." Archives of Biochemistry and Biophysics 537, no. 2:217-224. PNNL-SA-94926. doi:10.1016/j.abb.2013.07.015
• Buchko G.W., J. Abendroth, H. Robinson, Y. Zhang, S.N. Hewitt, T.E. Edwards, and W.C. Van Voorhis, et al. 2013. "Crystal structure of a macrophage migration inhibitory factor from Giardia lamblia." Journal of Structural and Functional Genomics 14, no. 2:47-57. PNNL-SA-93510. doi:10.1007/s10969-013-9155-9
• Buchko G.W., S.N. Hewitt, W.C. Van Voorhis, and P.J. Myler. 2013. "Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia." Journal of Biomolecular NMR 57, no. 4:369-374. PNWD-SA-10196. doi:10.1007/s10858-013-9797-8
• Lu J., Y. Xu, G.W. Buchko, and W.J. Shaw. 2013. "Mineral Association Changes the Secondary Structure and Dynamics of Murine Amelogenin." Journal of Dental Research 92, no. 11:1000-1004. PNNL-SA-94602. doi:10.1177/0022034513504929
• Sagaram U.S., K. El-Mounadi, G.W. Buchko, H.R. Berg, J. Kaur, R. Pandurangi, and T.J. Smith, et al. 2013. "Structural and functional studies of a phosphatidic acid-binding antifungal plant defensin MtDef4: Identification of an RGFRRR motif governing fungal cell entry." PLoS One 8, no. 12:e82485. PNNL-SA-90528. doi:10.1371/journal.pone.0082485
• Zhang Y., A. Gardberg, T.E. Edwards, B. Sankaran, H. Robinson, S.M. Varnum, and G.W. Buchko. 2013. "Structural Insights into the Functional Role of the Hcn Sub-domain of the Receptor-Binding Domain of the Botulinum Neurotoxin Mosaic Serotype C/D." Biochimie 95, no. 7:1379-1385. PNNL-SA-90823. doi:10.1016/j.biochi.2013.03.006

2012

• Buchko G.W., and H. Robinson. 2012. "Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family." FEBS Letters 586, no. 4:350-355. PNNL-SA-84898. doi:10.1016/j.febslet.2012.01.037
• Buchko G.W., H. Kim, P.J. Myler, T.C. Terwilliger, and C.Y. Kim. 2012. "Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis." Biomolecular NMR Assignments 6, no. 1:43-46. PNWD-SA-9329. doi:10.1007/s12104-011-9322-5
• Buchko G.W., I. Phan, I. Phan, L. Cron, R. Stacy, R. Stacy, and L.J. Stewart, et al. 2012. "Behind Every Good Metabolite there is a Great Enzyme (and perhaps a structure)." Metabolomics 2, no. 6:Article No. e124. PNNL-SA-91649.
• Jain A., G.W. Buchko, M.L. Reback, M.J. O'Hagan, B. Ginovska-Pangovska, J.C. Linehan, and W.J. Shaw. 2012. "Active Hydrogenation Catalyst with a Structured, Peptide-Based Outer-Coordination Sphere." ACS Catalysis 2, no. 10:2114-2118. PNNL-SA-88862. doi:10.1021/cs3004177
• Jin H., Y. Zhang, G.W. Buchko, S.M. Varnum, H. Robinson, T.C. Squier, and P.E. Long. 2012. "Structure Determination and Functional Analysis of a Chromate Reductase from Gluconacetobacter hansenii." PLoS One 7, no. 8:Article No. e42432. PNNL-SA-83740. doi:10.1371/journal.pone.0042432

2011

• Buchko G.W. 2011. "Structural genomics - A goldmine of blueprints for structure-based drug design." Metabolomics 1, no. 2:104e. PNWD-SA-9545. doi:10.4172/2153-0769.1000104e
• Buchko G.W., I. Phan, P.J. Myler, T.C. Terwilliger, and C.Y. Kim. 2011. "Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c." Archives of Biochemistry and Biophysics 506, no. 2:150-156. PNWD-SA-9015. doi:10.1016/j.abb.2010.12.001
• Buchko G.W., S.N. Hewitt, A.J. Napuli, W.C. Van Voorhis, and P.J. Myler. 2011. "Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis." Acta Crystallographica. Section F 67, no. 9:1129-1136. PNWD-SA-9253. doi:10.1107/S1744309111006336
• Buchko G.W., S.N. Hewitt, A.J. Napuli, W.C. Van Voorhis, and P.J. Myler. 2011. "Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis." Acta Crystallographica. Section F 67, no. 9:1148-1153. PNWD-SA-9241. doi:10.1107/S1744309111008189
• Buchko G.W., T.E. Edwards, J. Abendroth, T.L. Arakaki, L. Law, A.J. Napuli, and S.N. Hewitt, et al. 2011. "Structure of a Nudix hydrolase (MutT) in the Mg2+ -bound state from Bartonella henselae, the bacterium responsible for cat scratch fever." Acta Crystallographica. Section F 67, no. 9:1078-1083. PNWD-SA-9252. doi:10.1107/S1744309111011559
• Stacy R., R. Stacy, D.W. Begley, I. Phan, B.L. Staker, W.C. Van Voorhis, and G. Varani, et al. 2011. "Structural genomics of infectious disease drug targets: the SSGCID." Acta Crystallographica. Section F 67, no. 9:979-984. PNWD-SA-9280. doi:10.1107/S1744309111029204
• Zhang Y., G.W. Buchko, L. Qin, H. Robinson, and S.M. Varnum. 2011. "Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions." Biochemical and Biophysical Research Communications 404, no. 1:407-412. PNNL-SA-76463. doi:10.1016/j.bbrc.2010.11.134

2010

• Buchko G.W. 2010. "Circular Dichrosim Studies on the Deinococcus Radiodurans Nudix Hydrolase DR_0079: an Atypical Thermal Melt." Protein and Peptide Letters 17, no. 7:831-835. PNNL-SA-46812.
• Buchko G.W., B.J. Tarasevich, J. Roberts, M.L. Snead, and W.J. Shaw. 2010. "A Solution NMR Investigation into the Murine Amelogenin Splice-Variant LRAP (Leucine-Rich Amelogenin Protein)." Biochimica et Biophysica Acta--Proteins and Proteomics 1804, no. 9:1768-1774. PNNL-SA-69686.
• Buchko G.W., C.Y. Kim, T.C. Terwilliger, and P.J. Myler. 2010. "Solution Structure of Rv2377c-Founding Member of the MbtH-Like Protein Family." Tuberculosis 90, no. 4:245-251. PNWD-SA-8831.
• Buchko G.W., G. Niemann, E.S. Baker, M.E. Belov, R.D. Smith, F. Heffron, and J.N. Adkins, et al. 2010. "A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins." Molecular Biosystems 6, no. 12:2448-2458. PNNL-SA-73691. doi:10.1039/c0mb00097c
• Buchko G.W., H. Robinson, J. Abendroth, B.L. Staker, and P.J. Myler. 2010. "Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): Profound asymmetry in the crystal structure of the ‘open’ state." Biochemical and Biophysical Research Communications 394, no. 4:1012-1017. PNWD-SA-8859.
• Tang Z., H. Wu, J.R. Cort, G.W. Buchko, Y. Zhang, Y. Shao, and I.A. Aksay, et al. 2010. "Constraint of DNA on Functionalized Graphene Improves Its Biostability and Specificity." Small 6, no. 11:1205-1209. PNNL-SA-67870. doi:10.1002/smll.201000024
• Zhang Y., G.W. Buchko, L. Qin, H. Robinson, and S.M. Varnum. 2010. "Structural analysis of the receptor binding domain of botulinum neurotoxin serotype D." Biochemical and Biophysical Research Communications 401. PNNL-SA-75114. doi:10.1016/j.bbrc.2010.09.063
• Zhang Y., X. Gao, L. Qin, G.W. Buchko, H. Robinson, and S.M. Varnum. 2010. "High-level expression, purification, crystallization and preliminary X-ray crystallographic studies of the receptor binding domain of botulinum neurotoxin serotype D." Acta Crystallographica. Section F 66, no. 12:1610-1613. PNNL-SA-74543. doi:10.1107/S1744309110039874

2009

• Buchko G.W. 2009. "Pentapeptide Repeat Proteins and Cyanobacteria." In Handbook on Cyanobacteria: Biochemistry, Biotechnology and Applications. 233-257. Hauppauge, New York:Nova Science Publishers. PNNL-SA-62778.
• Buchko G.W., H. Robinson, and A. Addlagatta. 2009. "Structural characterization of the protein cce_0567 from Cyanothece 51142, a metalloprotein associated with nitrogen fixation in the DUF683 family." Biochimica et Biophysica Acta--Proteins and Proteomics 1794, no. 4:627-633. PNNL-SA-61462.
• Buchko G.W., S.N. Hewitt, A.J. Napuli, W.C. Van Voorhis, and P.J. Myler. 2009. "Backbone and side chain 1H, 13C, and 15N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei." Biomolecular NMR Assignments 3, no. 2:163-166. PNWD-SA-8472. doi:10.1007/s12104-009-9165-5
• Harvey S.D., G.W. Buchko, R.B. Lucke, C.W. Wright, A.M. Melville, A.J. Scott, and B.W. Wright. 2009. "The Structure and Purity of a Reference Dye Standard used for Quantification of C.I. Solvent Red 164 in Fuels." Dyes and Pigments 82, no. 3:307-315. PNNL-SA-59681. doi:10.1016/j.dyepig.2009.01.015
• Myler P.J., R. Stacy, R. Stacy, L.J. Stewart, B.L. Staker, W.C. Van Voorhis, and G. Varani, et al. 2009. "The Seattle Structure Genomics Center for Infectious Disease (SSGCID)." Infectious Disorders Drug Targets 9, no. 5:493-506. PNWD-SA-8486.
• Webb-Robertson B.M., L.A. McCue, N. Beagley, J.E. McDermott, D.S. Wunschel, S.M. Varnum, and J.Z. Hu, et al. 2009. "A Bayesian Integration Model of High-Throughput Proteomics and Metabolomics Data for Improved Early Detection of Microbial Infections." In Pacific Symposium on Biocomputing, 14, 451-463. Singapore:World Scientific Publishing Co. PNNL-SA-61531.

2008

• Buchko G.W., and H.J. Sofia. 2008. "Backbone 1H, 13C, and 15N NMR assignments for the Cyanothece 51142 protein cce_0567: a protein associated with nitrogen fixation in the DUF683 family." Biomolecular NMR Assignments 2. PNNL-SA-57687.
• Buchko G.W., B.J. Tarasevich, J.G. Bekhazi, M.L. Snead, and W.J. Shaw. 2008. "A Solution NMR Investigation into the Early Events of Amelogenin Nanosphere Self-Assembly Initiated with Sodium Chloride or Calcium Chloride." Biochemistry 47, no. 50:13215-13222. PNNL-SA-61196. doi:10.1021/bi8018288
• Buchko G.W., H. Robinson, H.B. Pakrasi, and M.A. Kennedy. 2008. "Insights into the structural variation between pentapeptide repeat proteins - Crystal structure of Rfr23 from Cyanothece 51142." Journal of Structural Biology 162, no. 1:184-192. PNNL-SA-54391.
• Buchko G.W., J.G. Bekhazi, J.R. Cort, N.B. Valentine, M.L. Snead, and W.J. Shaw. 2008. "1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein." Biomolecular NMR Assignments 2, no. 1:89-91. PNNL-SA-59235.
• Buchko G.W., O. Litvinova, H. Robinson, A.F. Yakunin, and M.A. Kennedy. 2008. "Functional and structural characterization of DR_0079 from Deinococcus radiodurans, a novel Nudix hydrolase with a preference for cytosine (deoxy) ribonucleoside 5'-di- and triphosphates." Biochemistry 47, no. 25:6571-82. PNNL-SA-58409.

2007

• Buchko G.W., S. Ni, N.M. Lourette, R.C. Reeves, and M.A. Kennedy. 2007. "NMR resonance assignments of the human high mobility group protein HMGA1." Journal of Biomolecular NMR 38, no. 2:185. PNNL-SA-51586. doi:10.1007/s10858-006-9116-8

2006

• Buchko G.W., and J. Cadet. 2006. "Identification of the a and ß Anomers of 1-(2-Deoxy-D-Erythro-Pentofuranosyl)-Oxaluric Acid at the Site of Riboflavin-mediated Photooxidation of Guanine in 2'-Deoxyguanosine and Thymidylyl-(3'-5')-2'-Deoxyguanosine." Photochemistry and Photobiology 82, no. 1:191-199. PNNL-SA-45422.
• Buchko G.W., C.Y. Kim, T.C. Terwilliger, and M.A. Kennedy. 2006. "Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis." Journal of Bacteriology 188, no. 16:5993-6001. PNNL-SA-46805. doi:10.1128/JB.00460-06
• Buchko G.W., H. Robinson, S. Ni, H.B. Pakrasi, and M.A. Kennedy. 2006. "Cloning, expression, crystallization and preliminary crystallographic analysis of a pentapeptide-repeat protein (Rfr23) from bacterium Cyanothece 511421." Acta Crystallographica. Section F 62, no. 12:1251-1254. PNNL-SA-51669. doi:10.1107/S174430910604663X
• Buchko G.W., S. Ni, H. Robinson, E.A. Welsh, H.B. Pakrasi, and M.A. Kennedy. 2006. "Characterization of two potentially universal turn motifs that shape the repeated five-residues fold - Crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142." Protein Science 15, no. 11:2579-2595. PNNL-SA-49580.

2005

• Buchko G.W., K. McAteer, S.S. Wallace, and M.A. Kennedy. 2005. "Solution-state NMR Investigation of DNA Binding Interactions in Escherichia coli Formamidopyrimidine-DNA Glycosylase (Fpg): A Dynamic Description of the DNA/Protein Interface." DNA Repair 4, no. 3:327-339. PNNL-SA-43028.

2004

• Buchko G.W., S. Ni, S.R. Holbrook, and M.A. Kennedy. 2004. "Solution Structure of Hypothetical Nudix Hydrolase DR0079 from Extremely Radiation-Resistant Deinococcus radiodurans Bacterium." Proteins. Structure, Function, and Bioinformatics 56, no. 1:28-39. PNWD-SA-6181.
• McAteer K., A. Aceves Gaona, R. Michalczyk, G.W. Buchko, N.G. Isern, L.A. Silks, and J.H. Miller, et al. 2004. "Compensating Bends in a 16 base-pair DNA Oligomer Containing a T3A3 Segment: A NMR Study of Global DNA Curvature." Biopolymers 75, no. 6:497-511. PNNL-SA-41115.

2003

• Buchko G.W., S. Ni, S.R. Holbrook, and M.A. Kennedy. 2003. "H-1, C-13, and N-15 NMR assignments of the hypothetical Nudix protein DR0079 from the extremely radiation-resistant bacterium Deinococcus radiodurans." Journal of Biomolecular NMR 25, no. 2:169-170. PNNL-SA-37579.
• Daughdrill G.W., G.W. Buchko, M.V. Botuyan, C.H. Arrowsmith, M.S. Wold, M.A. Kennedy, and D.F. Lowry. 2003. "Chemical shift changes provide evidence for overlapping single-stranded DNA and XPA binding sites on the 70 kDa subunit of human replication protein A." Nucleic Acids Research 31, no. 14:4176-4183. PNNL-SA-38556.
• Holbrook E.L., U. Schulze-Gahmen, G.W. Buchko, S. Ni, M.A. Kennedy, and S.R. Holbrook. 2003. "Purification, crystallization and preliminary X-ray analysis of two Nudix hydrolases from Deinococcus radiodurans." Acta Crystallographica. Section D, Biological Crystallography 59, no. Pt.4:737-740. PNNL-SA-37353.

2002

• Buchko G.W., and M. Weinfeld. 2002. "DNA-Targeted 2-Nitroimidazoles: Studies of the Influence of the Phenanthridine-Linked Nitroimidazoles, 2-NLP-3 and 2-NLP-4, on DNA Damage Induced by Ionizing Radiation." Radiation Research 158, no. 3:302-310. PNWD-SA-5465.
• Buchko G.W., S.S. Wallace, and M.A. Kennedy. 2002. "Base excision repair: NMR backbone assignments of Escherichia coli formamidopyrimidine-DNA glycosylase." Journal of Biomolecular NMR 22, no. 3:301-302. PNNL-SA-35528.

2001

• Buchko G.W., and M.A. Kennedy. 2001. "Hydroxyapatite Elution Behavior of Human Nucleotide Excision Repair Protein XPA and Fragments of XPA." Protein and Peptide Letters 8 (5), no. 2001:357-365. PNNL-SA-34760.
• Buchko G.W., C. Tung, K. Mcateer, N.G. Isern, L.D. Spicer, and M.A. Kennedy. 2001. "DNA-XPA Interactions: A 31P NMR Study of dCCAATAACC Association With the Minimal DNA-Binding Domain (M98-F219) of the Nucleotide Excision Repair Protein XPA." Nucleic Acids Research 29, no. 12:2635-2643. PNNL-SA-34180.
• Buchko G.W., N.G. Isern, L.D. Spicer, and M.A. Kennedy. 2001. "Human Nucleotide Excision Repair Protein XPA: NMR Spectroscopic Studies of an XPA Fragment Containing the ERCC1-Binding Region and the Minimal DNA-Binding Domain (M59-F219)." Mutation Research 486, no. 1:1-10. PNNL-SA-33784.
• Lipton A.S., G.W. Buchko, J.A. Sears, M.A. Kennedy, and P.D. Ellis. 2001. "Zn-67 Solid-State NMR Spectroscopy of the Minimal DNA Binding Domain of Human Nucleotide Excision Repair Protein XPA." Journal of the American Chemical Society 123, no. 5:992-993. PNWD-SA-5156.

2000

• Buchko G.W., A. Rozek, P. Kanda, M.A. Kennedy, and R.J. Cushley. 2000. "Structural Studies of a Baboon (Papio sp.) Plasma Protein Inhibitor of Cholesteryl Ester Transferase." Protein Science 9. PNNL-SA-32303.
• Buchko G.W., N.J. Hess, and M.A. Kennedy. 2000. "Cadmium Mutagenicity and Human Nucleotide Excision Repair Protein XPA: CD, EXAFS, and 1H/15N NMR Spectroscopic Studies on the Zinc (II) and Cadmium (II) Associated Minimal DNA-Binding Domain." Carcinogenesis 21, no. 5:1051-1057. PNNL-SA-31519.
• Buchko G.W., N.J. Hess, and M.A. Kennedy. 2000. "Human Nucleotide Excision Repair Protein XPA: Summary of EXAFS Studies On the Zn (II), Co (II), and Cd (II) Associated Minimal DNA-Binding Domain." Protein and Peptide Letters 7, no. 1:49-56. PNNL-SA-32501.
• Buchko G.W., N.J. Hess, V. Bandaru, S.S. Wallace, and M.A. Kennedy. 2000. "Spectroscopic Studies of Zinc (II) and Cobalt (II) Associated Escherichia Coli Formamidopyrimidine-DNA Glycosylase: Extended X-Ray Absorption Fine Structure Evidence for a Metal-Binding Domain." Biochemistry 39. PNNL-SA-33227.

1999

• Buchko G.W., G.W. Daughdrill, R. De Lorimier, S. Rao B K, N.G. Isern, J.M. Lingbeck, and J.S. Taylor, et al. 1999. "Interactions of Human Nucleotide Excision Repair Protein XPA with DNA and RPA70 Delta c327: Chemical Shift Mapping and N-15 NMR Relaxation Studies." Biochemistry 38, no. 46:15116-15128. PNNL-SA-32487.
• Buchko G.W., L.M. Iakoucheva, M.A. Kennedy, E.J. Ackerman, and N.J. Hess. 1999. "Extended X-ray Absorption Fine Structure Evidence for a Single Metal Binding Domain in Xenopus Laevis Nucleotide Excision Repair Protein XPA." Biochemical and Biophysical Research Communications 254, no. 1:109-113. PNNL-SA-30414.

1998

• Buchko G.W., A. Rozek, D.W. Hoyt, R.J. Cushley, and M.A. Kennedy. 1998. "The Use of Sodium Dodecyl Sulfate To Model the Apolipoprotein Environment. Evidence for Peptide-SDS Complexes Using Pulsed-Field-Gradient NMR Spectroscopy." Biochimica et Biophysica Acta--Lipids and Lipid Metabolism 1392, no. 1:101-108. PNNL-SA-28911. doi:10.1016/S0005-2760(98)00028-9
• Buchko G.W., S. Ni, B.D. Thrall, and M.A. Kennedy. 1998. "Structural Features of the Minimal DNA Binding Domain (M98-F219) of Human Nucleotide Excision Repair Protein XPA." Nucleic Acids Research 26, no. 11:2779-2788. PNNL-SA-29588.
• Hess N.J., G.W. Buchko, S. Ni, B.D. Thrall, M.A. Kennedy, S.D. Conradson, and F.J. Espinosa, et al. 1998. "Human Nucleotide Excision Repair Protein XPA: Extended X-ray Absorption Fine-Structure Evidence for a Metal-Binding Domain." Protein Science 7, no. 9:1970-1975. PNNL-SA-29836. doi:10.1002/pro.5560070912

1997

• Buchko G.W., and M.A. Kennedy. 1997. "Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a syntheic peptide fragment corresponding to the zinc-binding domain (101-141)." Journal of Biomolecular Structure and Dynamics 14, no. 6:677-690. PNNL-SA-28741. doi:10.1080/07391102.1997.10508171
• Buchko G.W., S. Ni, B.D. Thrall, and M.A. Kennedy. 1997. "Human Nucleotide Excision Repair Protein XPA: Expression and NMR Backbone Assignments of the 14.7 kDa Minimal Damaged DNA Binding Domain (Met98-Phe219)." Journal of Biomolecular NMR 10, no. 3:313-314. PNNL-SA-29061. doi:10.1023/A:1018321319578