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Crystallization and preliminary X‐ray diffraction studies of the cartilage link protein from bovine trachea
Author(s) -
Jedrzejas Marek J.,
Baker John R.,
Luo Ming
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.340220112
Subject(s) - crystallization , crystallography , chemistry , x ray crystallography , cartilage , protein crystallization , divalent , resolution (logic) , molecular mass , diffraction , anatomy , biology , enzyme , biochemistry , physics , optics , organic chemistry , artificial intelligence , computer science
Cartilage extracellular matrix link protein, having molecular mass of approximately 40 kDa, is a metalloprotein that binds divalent cations and is only soluble in low ionic strength solutions. The link protein was purified from bovine trachea and has been crystallized by a vapor diffusion method using PEG 3350 as precipitant. The crystal symmetry is P 1, and the unit cell dimensions are a = 43.55, b = 53.11, c = 60.10 Å, α = 90.44, β = 106.21, γ = 101.51°. The V M of 1.8 Å 3 /Da is consistent with the presence of two molecules of the link protein in the asymmetric unit. The crystals diffract X‐rays from a synchrotron source to 1.7 Å resolution. © 1995 Wiley‐Liss, Inc.