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Garry Buchko

Garry Buchko

IO Prototype & Pilot
Pacific Northwest National Laboratory
PO Box 999
MSIN: K8-98
Richland, WA 99352


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. 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 component of the Seattle Structural Genomics Center for Infectious Disease (SSGCID,, 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)

PNNL Publications









  • Buchko GW, H Robinson, HB Pakrasi, and MA Kennedy. 2008. "Insights into the structural variation between pentapeptide repeat proteins - Crystal structure of Rfr23 from Cyanothece 51142." Journal of Structural Biology 162(1):184-192. 



  • Buchko GW, and J Cadet. 2006. "Identification of the a and 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(1):191-199. 





  • Buchko GW, 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 (3):302-310. 





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