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Updated: Jun 16, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5
Yook Wah Choi1, Sujit Dutta, Burtram C Fielding
1Cancer and Developmental Cell Biology Division, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Singapore 138673, Singapore.
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, alpha = beta = gamma = 90 degrees .
