Crystallization and preliminary X-ray analysis of methylthioribose-1-phosphate isomerase from Bacillus subtilis

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Haruka TamuraYasushi Kai

Abstract

Methylthioribose-1-phosphate isomerase (MtnA) from Bacillus subtilis, the first enzyme in the downstream section of the methionine-salvage pathway, was crystallized using the sitting-drop vapour-diffusion method. Crystals grew using ammonium sulfate as the precipitant at 293 K. They diffracted to 2.5 A at 100 K using synchrotron radiation and were found to belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2, c = 154.7 A. The asymmetric unit contains two molecules of MtnA, with a VM value of 2.4 A3 Da(-1) and a solvent content of 48%.

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Citations

Aug 11, 2007·Bioscience, Biotechnology, and Biochemistry·Yohtaro SaitoAkiho Yokota

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