Crystallization and Preliminary X-ray Analysis of C-reactive Protein from Rat

Crystals of C-reactive protein from rat have been grown both with and without calcium. Two major components of the protein have been resolved on the basis of their calcium-dependent fine specificity for monophosphate esters. Crystals grown without calcium are tetragonal, space group P 42 12 with uni...

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Veröffentlicht in:	Journal of molecular biology 1994-01, Vol.235 (2), p.767-771
Hauptverfasser:	Hopkins, Margaret, Flanagan, Pauline A., Bailey, Susan, Glover, Ian D., Myles, Dean A.A., Greenhough, Trevor J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences C-reactive protein C-Reactive Protein - chemistry Crystalline structure Crystallization Crystallography, X-Ray Fundamental and applied biological sciences. Psychology Glycoproteins Male Molecular biophysics pentraxin Proteins rat Rats Rats, Wistar Structure in molecular biology
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Beschreibung
Zusammenfassung:	Crystals of C-reactive protein from rat have been grown both with and without calcium. Two major components of the protein have been resolved on the basis of their calcium-dependent fine specificity for monophosphate esters. Crystals grown without calcium are tetragonal, space group P 42 12 with unit cell parameters a = b = 163·81(9)Å and c = 125·21(6)Å, and diffract X-rays to 3·0 Å resolution. The rotation function specifies a molecular 5-fold symmetry axis at 24° away from c in the (110) plane.
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.1994.1028