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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 12
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pubmed:dateCreated |
2006-3-2
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-11807258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-1512252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-15501829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-1747104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-7678431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-7814342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-8352747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-9048379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-9092630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-9095194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-9495770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-9620260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511229-9678587
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1039-42
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16511229-Carbohydrates,
pubmed-meshheading:16511229-Crystallography, X-Ray,
pubmed-meshheading:16511229-Escherichia coli,
pubmed-meshheading:16511229-Maltose,
pubmed-meshheading:16511229-Oligosaccharides,
pubmed-meshheading:16511229-Plasmids,
pubmed-meshheading:16511229-Protein Structure, Tertiary,
pubmed-meshheading:16511229-Substrate Specificity,
pubmed-meshheading:16511229-Sulfolobus solfataricus,
pubmed-meshheading:16511229-alpha-Glucosidases
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pubmed:year |
2005
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pubmed:articleTitle |
Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus.
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pubmed:affiliation |
Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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