Papers in the Biological Sciences


Date of this Version



Acta Cryst. (2005). F61, 1039–1042


Copyright 2005 International Union of Crystallography. All rights reserved


MalA is an _-glucosidase from the hyperthermophilic archaeon Sulfolobus

solfataricus. It belongs to glycoside hydrolase family 31, which includes several

medically interesting α-glucosidases. MalA and its selenomethionine derivative

have been overproduced in Escherichia coli and crystallized in four different

crystal forms. Microseeding was essential for the formation of good-quality

crystals of forms 2 and 4. For three of the crystal forms (2, 3 and 4) full data sets

could be collected. The most suitable crystals for structure determination are the

monoclinic form 4 crystals, belonging to space group P21, from which data sets

extending to 2.5 Å resolution have been collected. Self-rotation functions

calculated for this form and for the orthorhombic (P212121) form 2 indicate the

presence of six molecules in the asymmetric unit related by 32 symmetry.

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