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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 1(68), p. 53-55, 2011

DOI: 10.1107/s1744309111046082

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Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA fromShewanella oneidensisMR-1

Journal article published in 2011 by S. J. Tomanicek, A. Johs ORCID, M. S. Sawhney, L. Shi, L. Liang
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.