Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1.
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 P2(1), with unit-cell parameters a = 93.0, b = 246.0, c = 136.6 Å, α = 90, β = 97.8, γ = 90°. X-ray diffraction data were collected to a maximum resolution of 3.25 Å.
Environmental Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA. tomaniceksj@ornl.gov
S J
SJ
Tomanicek
A
A
Johs
M S
MS
Sawhney
L
L
Shi
L
L
Liang
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry*; D020592:Shewanella / Q000201:enzymology*
D001425:Bacterial Outer Membrane Proteins; D003574:Cytochrome c Group