Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Ernst HA 

PROVIDER: S-EPMC1978162 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Ernst Heidi Asschenfeldt HA   Willemoës Martin M   Lo Leggio Leila L   Leonard Gordon G   Blum Paul P   Larsen Sine S  

Acta crystallographica. Section F, Structural biology and crystallization communications 20051105 Pt 12


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.  ...[more]

Similar Datasets

| S-EPMC107019 | biostudies-literature
| S-EPMC6996347 | biostudies-literature
| S-EPMC22234 | biostudies-literature
| S-EPMC5023256 | biostudies-literature
| S-EPMC6360439 | biostudies-literature
| S-EPMC2740566 | biostudies-literature
| S-EPMC3624569 | biostudies-literature
| S-EPMC1428385 | biostudies-literature
| S-EPMC3325985 | biostudies-literature
| S-EPMC1175829 | biostudies-literature