Crystallization And Preliminary X-Ray Diffraction Study Of Riboflavin Synthase

Autor: Zdzislaw Wawrazak, Joseph C. Calabrese, Douglas B. Jordan, Paul V. Viitanen
Rok vydání: 2001
Předmět:
Zdroj: Protein & Peptide Letters. 8:69-73
ISSN: 0929-8665
Popis: 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.
Databáze: OpenAIRE