 |
|
Title
|
|
Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo.
|
|
|
Authors
|
|
J.L.Martin,
G.Waksman,
J.C.Bardwell,
J.Beckwith,
J.Kuriyan.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
230,
1097-1100.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|