Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5

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dc.contributor.authorChoi, Yook-Wah
dc.contributor.authorDutta, Sujit
dc.contributor.authorFielding, Burtram C.
dc.contributor.authorTan, Yee-Joo
dc.date.accessioned2014-01-05T20:25:39Z
dc.date.available2014-01-05T20:25:39Z
dc.date.issued2010
dc.description.abstractThe DEAD-box RNA helicase DDX5 is involved in many aspects of RNA processing and has been implicated in a number of cellular processes involving alteration of RNA secondary structure. The N-terminal region of DDX5, which contains the conserved domain 1 of the DEAD-box helicases, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of this region is reported. X-ray diffraction data were processed to a resolution of 2.7 A ° . The crystals belonged to space group I222, with unit-cell parameters a = 66.18, b = 73.80, c = 104.00 A ° , = = = 90 .en_US
dc.description.accreditationWeb of Scienceen_US
dc.identifier.citationChoi, Y., et al. (2010). Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5. Acta Crystallographica Section F, 66(2): 192-194en_US
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/10566/912
dc.language.isoenen_US
dc.privacy.showsubmitterfalse
dc.publisherInternational Union of Crystallographyen_US
dc.rightsCopyright International Union of Crystallography. This file may be freely used for educational purposes, as long as it is not altered in any way. Acknowledgement of the authors and the source is required.
dc.source.urihttp://dx.doi.org/10.1107/S1744309109052956
dc.status.ispeerreviewedtrue
dc.subjectExpressionen_US
dc.subjectPurificationen_US
dc.subjectCrystallizationen_US
dc.titleExpression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5en_US
dc.typeArticleen_US

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