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Crystallization And Preliminary X-Ray Diffraction Study Of Riboflavin Synthase

Authors :
Zdzislaw Wawrazak
Joseph C. Calabrese
Douglas B. Jordan
Paul V. Viitanen
Source :
Protein & Peptide Letters. 8:69-73
Publication Year :
2001
Publisher :
Bentham Science Publishers Ltd., 2001.

Abstract

Escherichia coli riboflavin synthase crystallizes at 22 C in the presence of 7-10percent by volume diglyme, 20-50 mM MgCl2 and pH 7.0. In this medium diffraction quality crystals are routinely obtained within 5 h and they are stable for 10 weeks. The crystals are orthogonal in space group P212121 with unit cell dimensions of a=52.4 A , b = 62.1 A, c = 218.8 A. A 97percent complete data set was collected at 2.1 A resolution.

Details

ISSN :
09298665
Volume :
8
Database :
OpenAIRE
Journal :
Protein & Peptide Letters
Accession number :
edsair.doi...........12ad8ad08ce7975625a05585beb76816