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Crystallization and preliminary crystallographic analysis of the N‐terminal two domain fragment of vascular cell adhesion molecule‐1 (VCAM‐1)
Author(s) -
Wang Jiahuai,
Pepinsky Blake,
Karpusas Michael,
Liu Jinhuan,
Osborn Laurelee
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.340200310
Subject(s) - molecule , crystallization , crystallography , vcam 1 , crystal (programming language) , crystal structure , chemistry , cell adhesion molecule , stereochemistry , cell adhesion , adhesion , biology , organic chemistry , computer science , immunology , programming language
A molecular fragment comprising the first two domains of the human vascular cell adhesion molecule‐l (VCAM‐l) has been crystallized by the vapor diffusion method. Two crystal forms have been examined by X‐ray analysis: One crystal form belongs to the space group C 2 with two molecules in the asymmetric unit and cell parameters: a = 122.1 Å, b = 48.9 Å, c = 73.4 Å, and β = 117.4°. The other crystal form belongs to the space group P 2 1 with one molecule in the asymmetric unit and cell parameters: a = 40.4 Å, b = 45.7 Å, c = 54.7 Å, and β = 100.5°. Diffraction data up to 1.9 Å resolution have been collected for the C 2 crystal form. © 1994 Wiley‐Liss, Inc.