Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5.
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 .
Choi
Yook Wah
YW
Cancer 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.
Dutta
Sujit
S
Fielding
Burtram C
BC
Tan
Yee Joo
YJ
D003460:Crystallization; D053487:DEAD-box RNA Helicases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D015870:Gene Expression; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; C506749:Ddx5 protein, human; D053487:DEAD-box RNA Helicases