Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus.
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.
Ernst
Heidi Asschenfeldt
HA
Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Denmark.
Willemoës
Martin
M
Lo Leggio
Leila
L
Leonard
Gordon
G
Blum
Paul
P
Larsen
Sine
S
D002241:Carbohydrates / Q000737:chemistry; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D008320:Maltose / Q000737:chemistry; D009844:Oligosaccharides / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D048229:Sulfolobus solfataricus / Q000378:metabolism*; D000520:alpha-Glucosidases / Q000737:chemistry*
D002241:Carbohydrates; D009844:Oligosaccharides; D008320:Maltose; D000520:alpha-Glucosidases