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

S. J. Tomanicek; A. Johs; M. S. Sawhney; L. Shi; L. Liang

doi:10.1107/S1744309111046082

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

S. J. Tomanicek, A. Johs, M. S. Sawhney, L. Shi, L. Liang

Biogeochemical Dynamics

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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 P2₁, with unit-cell parameters a = 93.0, b = 246.0, c = 136.6 Å, = 90, Β = 97.8, = 90°. X-ray diffraction data were collected to a maximum resolution of 3.25 Å.

Original language	English
Pages (from-to)	53-55
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	1
DOIs	https://doi.org/10.1107/S1744309111046082
State	Published - Jan 1 2012

Keywords

OmcA
dissimilatory metal-reducing bacteria
outer membrane decaheme c-type cytochrome

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10.1107/S1744309111046082

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

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 P21, with unit-cell parameters a = 93.0, b = 246.0, c = 136.6 {\AA}, = 90, Β = 97.8, = 90°. X-ray diffraction data were collected to a maximum resolution of 3.25 {\AA}.",

keywords = "OmcA, dissimilatory metal-reducing bacteria, outer membrane decaheme c-type cytochrome",

author = "Tomanicek, {S. J.} and A. Johs and Sawhney, {M. S.} and L. Shi and L. Liang",

year = "2012",

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doi = "10.1107/S1744309111046082",

language = "English",

volume = "68",

pages = "53--55",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1. / Tomanicek, S. J.; Johs, A.; Sawhney, M. S. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 68, No. 1, 01.01.2012, p. 53-55.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1

AU - Tomanicek, S. J.

AU - Johs, A.

AU - Sawhney, M. S.

AU - Shi, L.

AU - Liang, L.

PY - 2012/1/1

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N2 - 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 Å, = 90, Β = 97.8, = 90°. X-ray diffraction data were collected to a maximum resolution of 3.25 Å.

AB - 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 Å, = 90, Β = 97.8, = 90°. X-ray diffraction data were collected to a maximum resolution of 3.25 Å.

KW - OmcA

KW - dissimilatory metal-reducing bacteria

KW - outer membrane decaheme c-type cytochrome

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DO - 10.1107/S1744309111046082

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SN - 1744-3091

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SP - 53

EP - 55

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 1

ER -

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

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Keywords

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