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Crystallization and preliminary X‐ray crystallographic analysis of chitinase from barley seeds
Author(s) -
Song Hyun Kyu,
Hwang Kwang Yeon,
Kim Kyeong Kyu,
Suh Se Won
Publication year - 1993
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.340170113
Subject(s) - crystallization , monoclinic crystal system , crystallography , chitinase , crystal (programming language) , polyethylene glycol , x ray , crystal structure , materials science , solvent , x ray crystallography , crystallinity , chemistry , diffraction , optics , physics , enzyme , organic chemistry , computer science , programming language
Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P 2 1 , with unit cell parameters of a = 69.43 Å, b = 44.55 Å, c = 81.41 Å, and β = 111.95 Å. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass ( V M ) of 2.25 Å 3 /Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 Å with X‐rays from a rotating anode source and is very stable in the X‐ray beam. X‐ray data have been collected to better than 2.2 Å Bragg spacing from a native crystal. © 1993 Wiley‐Liss, Inc.