Expression and crystallization of DsbA from Staphylococcus aureus

Bacterial Dsb proteins catalyse the in vivo formation of disulfide bonds, a critical step in the stability and activity of many proteins. Most studies on Dsb proteins have focused on Gram‐negative bacteria and thus the process of oxidative folding in Gram‐positive bacteria is poorly understood. To h...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-11, Vol.63 (11), p.953-956
Main Authors: Heras, B., Kurz, M., Jarrott, R., Byriel, K. A., Jones, A., Thöny-Meyer, L., Martin, J. L.
Format: Article
Language:English
Subjects:
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization Communications
Crystallography, X-Ray
CRYSTALS
DIFFRACTION
DIFFUSION
disulfide catalysts
DsbA
IN VIVO
INTERFACES
MOLECULES
Protein Disulfide-Isomerases - biosynthesis
Protein Disulfide-Isomerases - classification
Protein Folding
PROTEINS
RESOLUTION
SOLVENTS
SPACE GROUPS
STABILITY
STAPHYLOCOCCUS
Staphylococcus aureus
Staphylococcus aureus - enzymology
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Summary:Bacterial Dsb proteins catalyse the in vivo formation of disulfide bonds, a critical step in the stability and activity of many proteins. Most studies on Dsb proteins have focused on Gram‐negative bacteria and thus the process of oxidative folding in Gram‐positive bacteria is poorly understood. To help elucidate this process in Gram‐positive bacteria, DsbA from Staphylococcus aureus (SaDsbA) has been focused on. Here, the expression, purification, crystallization and preliminary diffraction analysis of SaDsbA are reported. SaDsbA crystals diffract to a resolution limit of 2.1 Å and belong to the hexagonal space group P65 or P61, with unit‐cell parameters a = b = 72.1, c = 92.1 Å and one molecule in the asymmetric unit (64% solvent content).
ISSN:1744-3091
1744-3091
DOI:10.1107/S174430910704821X