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

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

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


MalA is an α-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.

Original languageEnglish (US)
Pages (from-to)1039-1042
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number12
StatePublished - 2005

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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