Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE)

Edeling, M. A., Guddat, L. W., Fabianek, R. A., Halliday, J. A., Jones, A., Thony-Meyer, L. and Martin, J. L. (2001) Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE). Acta Crystallographica Section D-Biological Crystallography, D57 9: 1293-1295. doi:10.1107/S0907444901009982

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Author Edeling, M. A.
Guddat, L. W.
Fabianek, R. A.
Halliday, J. A.
Jones, A.
Thony-Meyer, L.
Martin, J. L.
Title Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE)
Journal name Acta Crystallographica Section D-Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
Publication date 2001-01-01
Sub-type Article (original research)
DOI 10.1107/S0907444901009982
Open Access Status File (Publisher version)
Volume D57
Issue 9
Start page 1293
End page 1295
Total pages 3
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Collection year 2001
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
Abstract t Disulfide-bond (Dsb) proteins are a family of redox proteins containing a Cys-X-X-Cys motif. They are essential for disulfide-bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for cytochrome c maturation. Crystals of Bradyrhizobium japonicum CcmG have been obtained that diffract X-rays to 1.14 Angstrom resolution. The crystals are orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 35.1, b = 48.2, c = 90.2 Angstrom. Selenomethionine CcmG was expressed without using a methionine auxotroph or methionine-pathway inhibition and was purified without reducing agents.
Keyword Biochemical Research Methods
Biochemistry & Molecular Biology
Biophysics
Crystallography
Disulfide Bond Formation
Cytochrome-c Maturation
Escherichia-coli
Periplasmic Thioredoxin
Formation Invivo
In-vivo
Protein
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Wed, 15 Aug 2007, 01:43:41 EST