Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis.

Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Research Abstract Details 

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Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Abstract Text:

David Goldstone,Edward N Baker,Peter Metcalf,

Protein disulfide-bond formation is poorly understood in the pathogenic bacterium Mycobacterium tuberculosis. Rv2874 is the M. tuberculosis homologue of the disulfide-bond electron transporter DsbD from Escherichia coli. Both proteins share a core central transmembrane domain and a C-terminal thioredoxin domain. To investigate the possible role of Rv2874 in disulfide-bond formation in M. tuberculosis, the C-terminal domain of Rv2874 has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 109.7, b = 118.3, c = 122.9 A, and diffract to at least 3.0 A.

Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Publishing Authors By Initials

D Goldstone,EN Baker,P Metcalf,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Acta crystallographica. Section F, Structural biol

VOLUME: 61

Page Numbers: 243-5

Journal Abbreviation: Acta Crystallogr. Sect. F Stru

ISSN: 1744-3091

DAY: 1

MONTH: 02

YEAR: 2005

Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Information

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LANGUAGE: eng

NlmUniqueID: 101226117

Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis. Information

Substance Name: DipZ protein, E coli

Registry Number: EC 1.8.1.8

Grant and Affiliation Information for Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis.

AFFILIATION: School of Biological Science, University of Auckland, Auckland, New Zealand.

Country: England

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MEDLINETA: Acta Crystallogr Sect F Struct

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