Linked Life Data

11679753

Source:http://linkedlifedata.com/resource/pubmed/id/11679753

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2001-10-26
pubmed:abstractText
Uroporphyrinogen-III decarboxylase from Nicotiana tabacum is a plastidial enzyme involved in the biosynthesis of chlorophyll and haem. Sedimentation equilibrium with protein producing diffracting crystals clearly indicates that the enzyme is a homodimer under similar ionic strength conditions to those found in the chloroplast stroma. Additionally, dynamic light scattering reveals an ionic strength dependence for this oligomerization state. Crystals were obtained in the hexagonal space group P622 with one molecule per asymmetric unit and diffracted to 2.3 A resolution using synchrotron radiation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1709-11
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis.
pubmed:affiliation
Max-Planck-Institut für Biochemie, Abt. Strukturforschung, Am Klopferspitz 18-a, D-82152 Martinsried bei München, Germany. martins@biochem.mpg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't