Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.

Crystallization and preliminary crystallographic analysis of the phosphoglucose isomerase from a Bacillus subtilis native strain were carried out. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 145.7, b = 136.0, c = 109.1 A, beta = 119.4 degrees . The diffraction quality of the crystal was significantly improved from 2.4 A to greater than 1.9 A resolution by using the in situ flash-annealing method. A 98% complete data set with an overall R(merge) of 4.6% was collected using an R-AXIS IV(++) image-plate system and a copper rotating-anode X-ray generator. The crystals contained four molecules per asymmetric unit and the predicted solvent content and the Matthews coefficient (V(M)) were 46.8% and 2.3 A(3) Da(-1), respectively. Structure determination by the molecular-replacement method provided a reasonable solution for model building.