Crystallization And Preliminary X-Ray Diffraction Study Of Riboflavin Synthase

Authors: Wawrazak Z.; Viitanen P.V.; Calabrese J.C.; Jordan D.B.

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 69-73(5)

Publisher: Bentham Science Publishers

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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.

Keywords: RIBOFLAVIN SYNTHASE

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409698

Publication date: 2001-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.