Open AccessCharacterization of different crystal forms of the α‐glucosidase MalA from Sulfolobus solfataricus
Author(s) -
Ernst Heidi Asschenfeldt,
Willemoës Martin,
Lo Leggio Leila,
Leonard Gordon,
Blum Paul,
Larsen Sine
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105035177
Subject(s) - sulfolobus solfataricus , orthorhombic crystal system , monoclinic crystal system , crystallography , glycoside hydrolase , hydrolase , crystal (programming language) , space group , chemistry , crystal structure , stereochemistry , x ray crystallography , physics , diffraction , enzyme , archaea , biochemistry , optics , computer science , programming language , gene
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 P 2 1 , from which data sets extending to 2.5 Å resolution have been collected. Self‐rotation functions calculated for this form and for the orthorhombic ( P 2 1 2 1 2 1 ) form 2 indicate the presence of six molecules in the asymmetric unit related by 32 symmetry.