Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus
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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 language | English |
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Journal | Acta Crystallographica. Section F : Structural Biology and Crystallization Communications |
Volume | 61 |
Issue number | Pt 12 |
Pages (from-to) | 1039-42 |
Number of pages | 3 |
ISSN | 1744-3091 |
DOIs | |
Publication status | Published - 2005 |
Bibliographical note
Keywords: Carbohydrates; Crystallography, X-Ray; Escherichia coli; Maltose; Oligosaccharides; Plasmids; Protein Structure, Tertiary; Substrate Specificity; Sulfolobus solfataricus; alpha-Glucosidases
ID: 13132146