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|Title:||Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5||Authors:||Choi, Y.-W.
|Issue Date:||2010||Citation:||Choi, Y.-W., Dutta, S., Fielding, B.C., Tan, Y.-J. (2010). Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 66 (2) : 192-194. ScholarBank@NUS Repository. https://doi.org/10.1107/S1744309109052956||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 Å. The crystals belonged to space group I222, with unit-cell parameters a = 66.18, b = 73.80, c = 104.00 Å, α = β = γ = 90°. © 2010 International Union of Crystallography All rights reserved.||Source Title:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications||URI:||http://scholarbank.nus.edu.sg/handle/10635/109340||ISSN:||17443091||DOI:||10.1107/S1744309109052956|
|Appears in Collections:||Staff Publications|
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