Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo.
DsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a number of exported proteins in Escherichia coli. Crystals of oxidized DsbA have been obtained from polyethylene glycol 8000 (20 to 25%), 0.1 M-cacodylate buffer (pH 6.5) and 1% 2-methyl-2,4-pentanediol. Oxidation of the protein is critical for reproducibly obtaining high quality crystals. The resulting crystals diffract to 2 A and belong to the monoclinic space group C2 with cell dimensions a = 117.5 A, b = 65.0 A, c76.3 A, beta = 126.3 degrees with two molecules in the asymmetric unit.
Martin
J L
JL
Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.
Waksman
G
G
Bardwell
J C
JC
Beckwith
J
J
Kuriyan
J
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D004220:Disulfides / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry*; D007535:Isomerases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D004220:Disulfides; D007535:Isomerases; D019704:Protein Disulfide-Isomerases