Please use this identifier to cite or link to this item: https://doi.org/10.1107/S1744309109052956
Title: Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5
Authors: Choi, Y.-W.
Dutta, S.
Fielding, B.C.
Tan, Y.-J. 
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

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

1
checked on Jun 19, 2018

WEB OF SCIENCETM
Citations

1
checked on Jun 19, 2018

Page view(s)

46
checked on Jun 1, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.