Purification, crystallization and preliminary crystallographic studies on the N-terminal fragment of human protein disulfide isomerase.
A fragment of human protein disulfide isomerase composed of the thioredoxin-like a and b domains (ab) has been expressed in Escherichia coli as a fusion protein with glutathione-S-transferase and purified after thrombin cleavage. Two forms of ab crystal were obtained with polyethylene glycol as precipitant and different additives at pH 7.5. The space group of form I is P4(1)2(1)2 or P4(3)2(1)2, with unit-cell dimensions a = 81.5, c = 259.7 A. The space group of form II is P4(1)22 or P4(3)22, with unit-cell dimensions a = 82.7, c = 86.5 A.
Wang
X Q
XQ
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, People's Republic of China.
Gui
L L
LL
Dai
Y
Y
Wang
C C
CC
Chang
W R
WR
Liang
D C
DC
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry; D011092:Polyethylene Glycols; D019704:Protein Disulfide-Isomerases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013879:Thioredoxins / Q000737:chemistry
D010446:Peptide Fragments; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D013879:Thioredoxins; D019704:Protein Disulfide-Isomerases