Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1

Journal Article · Thu May 24 00:00:00 EDT 2012 · Acta Crystallogr. F

DOI:https://doi.org/10.1107/S1744309111046082· OSTI ID:1033434

Tomanicek, S J; Johs, A; Sawhney, M S; Shi, L; Liang, L ^[1]

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1. PNNL

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{sub 1}, with unit-cell parameters a = 93.0, b = 246.0, c = 136.6 {angstrom}, = 90, {beta} = 97.8, {gamma} = 90{sup o}. X-ray diffraction data were collected to a maximum resolution of 3.25 {angstrom}.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: DOE - BIOLOGICAL AND ENVIRONMENTAL RESEARCH
• OSTI ID: 1033434
• Journal Information: Acta Crystallogr. F, Vol. 68, Issue (1) ; 01, 2012; ISSN 1744-3091
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
BINDING ENERGY
CRYSTALLIZATION
CYTOCHROMES
ELECTRONS
MEMBRANES
OXIDOREDUCTASES
RESOLUTION
SPACE GROUPS
VALENCE
X-RAY DIFFRACTION