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 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 A and belong to the hexagonal space group P6(5) or P6(1), with unit-cell parameters a = b = 72.1, c = 92.1 A and one molecule in the asymmetric unit (64% solvent content).
Heras
B
B
Institute for Molecular Bioscience and ARC Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane QLD 4072, Australia. b.heras@imb.uq.edu.au
Kurz
M
M
Jarrott
R
R
Byriel
K A
KA
Jones
A
A
Thöny-Meyer
L
L
Martin
J L
JL
D003460:Crystallization; D018360:Crystallography, X-Ray; D019704:Protein Disulfide-Isomerases / Q000096:biosynthesis* / Q000145:classification*; D017510:Protein Folding; D013211:Staphylococcus aureus / Q000201:enzymology*
D019704:Protein Disulfide-Isomerases