pubmed-article:16511229 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16511229 | lifeskim:mentions | umls-concept:C0995927 | lld:lifeskim |
pubmed-article:16511229 | lifeskim:mentions | umls-concept:C0002272 | lld:lifeskim |
pubmed-article:16511229 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:16511229 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:16511229 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:16511229 | pubmed:issue | Pt 12 | lld:pubmed |
pubmed-article:16511229 | pubmed:dateCreated | 2006-3-2 | lld:pubmed |
pubmed-article:16511229 | 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. | lld:pubmed |
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pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:language | eng | lld:pubmed |
pubmed-article:16511229 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16511229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16511229 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16511229 | pubmed:month | Dec | lld:pubmed |
pubmed-article:16511229 | pubmed:issn | 1744-3091 | lld:pubmed |
pubmed-article:16511229 | pubmed:author | pubmed-author:LarsenSineS | lld:pubmed |
pubmed-article:16511229 | pubmed:author | pubmed-author:Lo... | lld:pubmed |
pubmed-article:16511229 | pubmed:author | pubmed-author:LeonardGordon... | lld:pubmed |
pubmed-article:16511229 | pubmed:author | pubmed-author:WillemoësMart... | lld:pubmed |
pubmed-article:16511229 | pubmed:author | pubmed-author:BlumPaulP | lld:pubmed |
pubmed-article:16511229 | pubmed:author | pubmed-author:ErnstHeidi... | lld:pubmed |
pubmed-article:16511229 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:16511229 | pubmed:day | 1 | lld:pubmed |
pubmed-article:16511229 | pubmed:volume | 61 | lld:pubmed |
pubmed-article:16511229 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16511229 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16511229 | pubmed:pagination | 1039-42 | lld:pubmed |
pubmed-article:16511229 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:16511229 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16511229 | pubmed:articleTitle | Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus. | lld:pubmed |
pubmed-article:16511229 | pubmed:affiliation | Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Denmark. | lld:pubmed |
pubmed-article:16511229 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16511229 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:1453070 | entrezgene:pubmed | pubmed-article:16511229 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16511229 | lld:entrezgene |