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Crystallization and preliminary X‐ray diffraction studies of dogfish C‐reactive protein
Author(s) -
Samudzi Cleopas T.,
Nguyen Nga Y.,
Rubin J. Ronald
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.340150112
Subject(s) - triclinic crystal system , ammonium sulfate , crystallization , crystallography , diffraction , x ray crystallography , chemistry , resolution (logic) , lattice (music) , crystal structure , materials science , chromatography , organic chemistry , optics , physics , artificial intelligence , computer science , acoustics
Crystals of dogfish ( Mustelus canis ) C‐reactive protein were obtained through vapor phase equilibration using the sitting drop rod technique with ammonium sulfate as the precipitating agent. The space group was determined to be P 1 (triclinic lattice) with unit cell dimensions of a = 82.91, b = 92.25 and c = 103.40 Å; α = 83.36°, β = 89.76°, and γ = 81.30°. These crystals diffract to about 2.6 Å resolution and contain two hexamers in the asymmetric unit. © 1993 Wiley‐Liss, Inc.