Crystallization and preliminary X-ray analysis of the 6-phospho-α-glucosidase from Bacillus subtilis
1999 ◽
Vol 55
(6)
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pp. 1212-1214
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Keyword(s):
X Ray
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6-Phospho-α-glucosidase (GlvA) is the protein involved in the dissimilation of α-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS) in Bacillus subtilis. The purified enzyme 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 presence of manganese and NAD. They diffract beyond 2.2 Å using synchrotron radiation and belong to the space group I222 (or its enantiomorph) with unit-cell dimensions a = 83.26, b = 102.56, c = 145.31 Å and contain a single molecule of GlvA in the asymmetric unit.
1999 ◽
Vol 55
(7)
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pp. 1353-1355
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