Premium
Microtube batch protein crystallization: Applications to human immunodeficiency virus type 2 (HIV‐2) protease and human renin
Author(s) -
Pav Susan,
Lubbe Klaus,
Dô Florence,
Lamarre Daniel,
Pargellis Christopher,
Tong Liang
Publication year - 1994
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.340200110
Subject(s) - crystallization , protease , recombinant dna , human immunodeficiency virus (hiv) , protein crystallization , renin–angiotensin system , chemistry , enzyme , materials science , combinatorial chemistry , virology , biochemistry , biology , organic chemistry , blood pressure , gene , endocrinology
For therapeutically relevant targets, the evaluation of enzymes in complex with their inhibitors by cocrystallization and high resolution structural analysis has become a vital component of structure‐driven drug design and development. Two approaches, hanging drop vapor diffusion and a novel microtube batch method, were utilized in parallel to grow crystals of recombinant HIV ‐2 protease and recombinant human renin in complex with inhibitors. In the case of HIV ‐2 protease in complex with a reduced amide inhibitor, crystallization was achieved only by the microbatch method. In the case of human renin, the addition of precipitant was required for crystal growth. The microbatch method described here is a useful supplementary or alternative approach for screening parameters and generating crystals suitable for high resolution structural analysis. © 1994 Wiley‐Liss, Inc.