Crystallization and preliminary X-ray analysis of the 6-phospho-alpha-glucosidase from Bacillus subtilis

6-Phospho-alpha-glucosidase (GIvA) is the protein involved in the dissimila tion of a-glycosides accumulated viaaphosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS) in Bacillus subtilis. The purified enzy me has been crystallized in a form suitable for X-ray diffraction analysis. Thin rod-like crystals have been grown by the hanging-drop method in the p resence of manganese and NAD. They diffract beyond 22 Angstrom using synchr otron radiation and belong to the space group I222 (or its enantiomorph) wi th unit-cell dimensions a = 83.26, b = 102.56, c = 145.31 Angstrom and cont ain a single molecule of GIvA in the asymmetric unit.