| pubmed-article:11976500 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11976500 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11976500 | lifeskim:mentions | umls-concept:C0007035 | lld:lifeskim |
| pubmed-article:11976500 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
| pubmed-article:11976500 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:11976500 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:11976500 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
| pubmed-article:11976500 | pubmed:issue | Pt 5 | lld:pubmed |
| pubmed-article:11976500 | pubmed:dateCreated | 2002-4-26 | lld:pubmed |
| pubmed-article:11976500 | pubmed:abstractText | Carbonic anhydrases catalyze the interconversion of carbon dioxide to bicarbonate. Human carbonic anhydrase isozyme III with a C-terminal hexahistidine tag was overexpressed in Eschericha coli, purified and crystallized. Diffraction data (93.4% completeness) were collected to 2.2 A resolution on an in-house R-AXIS IV++ image-plate system with Osmic mirrors and a Rigaku HU-H3R CU rotating-anode generator operating at 50 kV and 100 mA. A 60 degrees sweep of data were collected from a single crystal with a crystal-to-detector distance of 150 mm and a 0.5 degrees oscillation angle per frame using an exposure of 60 s per frame at 293 K. The crystals were shown to conform to the Laue hexagonal crystal system P6, with unit-cell parameters a = 44.7, c = 222.5 A and a scaling R(sym) of 0.087 for 11 962 unique reflections. Using the known crystal structure of the rat form of carbonic anhydrase isozyme III, a molecular-replacement model was built. This model was used for rotation and translation searches and uniquely defined the space group as P6(5). Rigid-body refinement of the model was used to generate an initial phased electron-density map with an R(work) of 31.17%. | lld:pubmed |
| pubmed-article:11976500 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11976500 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11976500 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11976500 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11976500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11976500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11976500 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11976500 | pubmed:month | May | lld:pubmed |
| pubmed-article:11976500 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:TuChingkuangC | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:McKennaRobert... | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:SilvermanDavi... | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:AnHaiqianH | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:GovindasamyLa... | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:DudaDavid MDM | lld:pubmed |
| pubmed-article:11976500 | pubmed:author | pubmed-author:YoshiokaCraig... | lld:pubmed |
| pubmed-article:11976500 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11976500 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:11976500 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11976500 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11976500 | pubmed:pagination | 849-52 | lld:pubmed |
| pubmed-article:11976500 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:meshHeading | pubmed-meshheading:11976500... | lld:pubmed |
| pubmed-article:11976500 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11976500 | pubmed:articleTitle | Crystallization and preliminary X-ray analysis of human carbonic anhydrase III. | lld:pubmed |
| pubmed-article:11976500 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA. | lld:pubmed |
| pubmed-article:11976500 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11976500 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11976500 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:761 | entrezgene:pubmed | pubmed-article:11976500 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:11976500 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11976500 | lld:pubmed |
