2jgn: Difference between revisions

Revision as of 20:39, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jgn.png

Template:STRUCTURE 2jgn

DDX3 HELICASE DOMAINDDX3 HELICASE DOMAIN

Template:ABSTRACT PUBMED 17401195

About this StructureAbout this Structure

2JGN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain., Rodamilans B, Montoya G, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):283-6. Epub 2007 Mar 12. PMID:17401195

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''DDX3 HELICASE DOMAIN'''
+===DDX3 HELICASE DOMAIN===
-==Overview==
+<!--
-DDX3 is a human RNA helicase that is involved in RNA processing and important human diseases. This enzyme belongs to the DEAD-box protein family, the members of which are characterized by the presence of nine conserved motifs including the Asp-Glu-Ala-Asp motif that defines the family. DDX3 has two distinct domains: an ATP-binding domain in the central region of the protein and a helicase domain in the carboxy-terminal region. The helicase domain of DDX3 was cloned and overexpressed in Escherichia coli. Crystallization experiments yielded crystals that were suitable for X-ray diffraction analysis. The final crystallization conditions were a reservoir solution consisting of 2 M ammonium sulfate, 0.1 M imidazole pH 6.4 plus 5 mM spermine tetrahydrochloride and a protein solution containing 10 mM HEPES, 500 mM ammonium sulfate pH 8.0. The crystals of the helicase domain belong to the monoclinic space group P2(1), with unit-cell parameters a = 43.85, b = 60.72, c = 88.39 A, alpha = gamma = 90, beta = 101.02 degrees , and contained three molecules per asymmetric unit. These crystals diffracted to a resolution limit of 2.2 A using synchrotron radiation at the European Synchrotron Radiation Facility (ESRF) and the Swiss Light Source (SLS).
+The line below this paragraph, {{ABSTRACT_PUBMED_17401195}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17401195}}
 ==About this Structure==
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 [[Category: Phosphorylation]]
 [[Category: Rna-binding]]
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