The outer membrane cytochrome OmcA functions as a terminal metal reductase
in the dissimilatory metal-reducing bacterium Shewanella oneidensis MR-1. The
ten-heme centers shuttle electrons from the transmembrane donor complex
to extracellular electron acceptors. Here, the crystallization and preliminary
crystallographic analysis of OmcA are reported. Crystals of OmcA were grown
by the sitting-drop vapor-diffusion method using PEG 20 000 as a precipitant.
The OmcA crystals belonged to space group P21, with unit-cell parameters
a = 93.0, b = 246.0, c = 136.6 A ° , * = 90, * = 97.8, * = 90*. X-ray diffraction data
were collected to a maximum resolution of 3.25 A ° .
Revised: February 22, 2013 |
Published: January 1, 2012
Citation
Tomanicek S.J., A. Johs, M.S. Sawhney, L. Shi, and L. Liang. 2012.Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1.Acta Crystallographica. Section F 68, no. 1:53-55.PNNL-SA-85682.doi:10.1107/S1744309111046082