Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus

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Heidi Asschenfeldt Ernst, Martin Willemoës, Leila Lo Leggio, Gordon Leonard, Paul Blum, Sine Larsen

MalA is an alpha-glucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. It belongs to glycoside hydrolase family 31, which includes several medically interesting alpha-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 P2(1), from which data sets extending to 2.5 A resolution have been collected. Self-rotation functions calculated for this form and for the orthorhombic (P2(1)2(1)2(1)) form 2 indicate the presence of six molecules in the asymmetric unit related by 32 symmetry.
Original languageEnglish
JournalActa Crystallographica. Section F : Structural Biology and Crystallization Communications
Issue numberPt 12
Pages (from-to)1039-42
Number of pages3
Publication statusPublished - 2005

Bibliographical note

Keywords: Carbohydrates; Crystallography, X-Ray; Escherichia coli; Maltose; Oligosaccharides; Plasmids; Protein Structure, Tertiary; Substrate Specificity; Sulfolobus solfataricus; alpha-Glucosidases

ID: 13132146