TY - JOUR
T1 - Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus
AU - Ernst, Heidi Asschenfeldt
AU - Willemoës, Martin
AU - Lo Leggio, Leila
AU - Leonard, Gordon
AU - Blum, Paul
AU - Larsen, Sine
N1 - Keywords: Carbohydrates; Crystallography, X-Ray; Escherichia coli; Maltose; Oligosaccharides; Plasmids; Protein Structure, Tertiary; Substrate Specificity; Sulfolobus solfataricus; alpha-Glucosidases
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
U2 - 10.1107/S1744309105035177
DO - 10.1107/S1744309105035177
M3 - Journal article
C2 - 16511229
SN - 2053-230X
VL - 61
SP - 1039
EP - 1042
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - Pt 12
ER -