Crystallization And Preliminary X-Ray Diffraction Study Of Riboflavin Synthase

Zdzislaw      Wawrazak; Paul   V.   Viitanen; Joseph   C.   Calabrese; Douglas   B.   Jordan

doi:10.2174/0929866013409698

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

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Protein & Peptide Letters

Title: Crystallization And Preliminary X-Ray Diffraction Study Of Riboflavin Synthase

Volume: 8 Issue: 1

Author(s): Zdzislaw Wawrazak, Paul V. Viitanen, Joseph C. Calabrese and Douglas B. Jordan

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Keywords: RIBOFLAVIN SYNTHASE

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.

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Wawrazak Zdzislaw, Viitanen V. Paul, Calabrese C. Joseph and Jordan B. Douglas, Crystallization And Preliminary X-Ray Diffraction Study Of Riboflavin Synthase, Protein & Peptide Letters 2001; 8 (1) . https://dx.doi.org/10.2174/0929866013409698