Crystallization and preliminary X‐ray diffraction studies of dogfish C‐reactive protein | Zendy

Samudzi Cleopas T. | Zendy; Nguyen Nga Y. | Zendy; Rubin J. Ronald | Zendy

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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.

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