Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6
pubmed:dateCreated
2006-3-2
pubmed:abstractText
Carbazole 1,9a-dioxygenase, which consists of an oxygenase component (CARDO-O) and the electron-transport components ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R), catalyzes dihydroxylation at the C1 and C9a positions of carbazole. The electron-transport complex between CARDO-O and CARDO-F crystallizes at 293 K using hanging-drop vapour diffusion with the precipitant PEG MME 2000 (type I crystals) or PEG 3350 (type II). Blossom-shaped crystals form from a pile of triangular plate-shaped crystals. The type I crystal diffracts to a maximum resolution of 1.90 A and belongs to space group P2(1), with unit-cell parameters a = 97.1, b = 89.8, c = 104.9 A, alpha = gamma = 90, beta = 103.8 degrees. Diffraction data for the type I crystal gave an overall Rmerge of 8.0% and a completeness of 100%. Its VM value is 2.63 A3 Da(-1), indicating a solvent content of 53.2%.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-10051560, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-10322011, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-10872075, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-11053423, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-11175898, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-11256611, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-11472938, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-12450109, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-12450807, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-12728980, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-15277751, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-15292119, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-15645447, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-2294093, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-2982815, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-5700707, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-7204373, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-7629085, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-8048958, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-9244274, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-942051, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511100-9650248
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
577-80
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Crystallization and preliminary X-ray diffraction analysis of the electron-transfer complex between the terminal oxygenase component and ferredoxin in the Rieske non-haem iron oxygenase system carbazole 1,9a-dioxygenase.
pubmed:affiliation
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't