Expression and crystallization of DsbA from Staphylococcus aureus.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 63(Pt 11): 953-6, 2007 Nov 01.
Article
in En
| MEDLINE
| ID: mdl-18007049
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).
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Staphylococcus aureus
/
Protein Disulfide-Isomerases
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2007
Document type:
Article