Premium
Crystallization and X‐ray diffraction data of the cleaved form of plasminogen activator inhibitor‐1
Author(s) -
Aertgeerts K.,
De Bondt H. L.,
De Ranter C.,
Declerck P. J.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230114
Subject(s) - crystallization , crystallography , chemistry , monoclinic crystal system , diffraction , x ray crystallography , molecule , plasminogen activator , cleavage (geology) , crystal structure , stereochemistry , materials science , physics , biology , optics , organic chemistry , fracture (geology) , composite material , endocrinology
To characterize the structural requirements for the conformational flexibility in plasminogen activator inhibitor‐1 (Pal‐1) we have crystallized human PAI‐1, carrying a mutation which stabilizes PAI‐1 in its substrate form. Crystallization was performed by the hanging drop diffusion method at pH 8.5 in the presence of 19% (w/v) polyethyleneglycol 4000 as a precipitant. The crystals appear after 3 days at 23°C and belong to the monoclinic space group C 2 with cell dimensions of a =151.8 Å, b =47.5 Å, c =62.7 Å, and β=113.9°, and one molecule in the asymmetric unit. The X‐ray diffraction data set contains data with a limiting resolution of 2.5 Å. Biochemical analysis of the redissolved crystals indicated that during the crystallization process, cleavage had occurred in the active site loop at the P1‐P1′ position. The availability of good‐quality crystals of the cleaved form of this serpin will allow its three‐dimensional structure to be solved and will provide detailed information on the structure‐function relationship in PAI‐1. © 1995 Wiley‐Liss, Inc.