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Crystallization and preliminary studies of lima bean trypsin inhibitor
Author(s) -
Samudzi Cleopas,
Schroeder Steven,
Griffith Scott,
Chen Xin,
Quinn Thomas P.
Publication year - 1997
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/(sici)1097-0134(199702)27:2<311::aid-prot16>3.0.co;2-p
Subject(s) - trypsin , crystallization , trypsin inhibitor , chemistry , biochemistry , enzyme , organic chemistry
Crystals of lima bean trypsin inhibitor (LBTI) were obtained by using the vapor phase equilibration technique with sodium/potassium tartrate as the precipitating agent. The space group was determined to be cubic, I2 1 3 with a = 110.2 Å. These crystals diffract to about 1.9 Å resolution. Preliminary analysis of self‐rotation maps (calculated from native x‐ray intensity data) suggests the presence of two monomers in the asymmetric unit. LBTI is very thermostable and retains activity even after boiling for 10 minutes. This property is exploited as part of its purification procedure. © 1997 Wiley‐Liss, Inc.