Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5
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Date
2010
Journal Title
Journal ISSN
Volume Title
Publisher
International Union of Crystallography
Abstract
The 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 .
Description
Keywords
Expression, Purification, Crystallization
Citation
Choi, Y., et al. (2010). Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5. Acta Crystallographica Section F, 66(2): 192-194