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

Phosphoglucose isomerase from B. subtilis has been purified and crystallized. The diffraction quality of the crystal was improved by using a flash-annealing technique and 1.9 Å resolution in-house X-ray data were collected. 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 Å, β = 119.4°. The diffraction quality of the crystal was significantly improved from 2.4 Å to greater than 1.9 Å 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 ų Da⁻¹, respectively. Structure determination by the molecular-replacement method provided a reasonable solution for model building