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Crystallization and preliminary X‐ray analysis of the RPB5 subunit of human RNA polymerase II

Crystallization and preliminary X‐ray analysis of the RPB5 subunit of human RNA polymerase II RPB5 is an essential subunit of eukaryotic RNA polymerase II. It has been proposed to interact with DNA and several key transcription factors during transcription. These interactions are crucial for transcription and its regulation. Here, prior to obtaining complex structures of human RPB5 and its binding partners, recombinant human RPB5 was crystallized alone by vapour diffusion in hanging drops. A complete data set was collected from a single frozen crystal employing an in‐house X‐ray source. The crystal diffracted to 2.8 Å resolution and belonged to space group P43212. The likely Matthews coefficient and solvent content of 2.67 Å3 Da−1 and 53.92%, respectively, suggested the presence of two protein subunits in the asymmetric unit. The structure was solved using molecular replacement. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray analysis of the RPB5 subunit of human RNA polymerase II

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References (32)

Publisher
Wiley
Copyright
International Union of Crystallography, 2011
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111033288
pmid
22102239
Publisher site
See Article on Publisher Site

Abstract

RPB5 is an essential subunit of eukaryotic RNA polymerase II. It has been proposed to interact with DNA and several key transcription factors during transcription. These interactions are crucial for transcription and its regulation. Here, prior to obtaining complex structures of human RPB5 and its binding partners, recombinant human RPB5 was crystallized alone by vapour diffusion in hanging drops. A complete data set was collected from a single frozen crystal employing an in‐house X‐ray source. The crystal diffracted to 2.8 Å resolution and belonged to space group P43212. The likely Matthews coefficient and solvent content of 2.67 Å3 Da−1 and 53.92%, respectively, suggested the presence of two protein subunits in the asymmetric unit. The structure was solved using molecular replacement.

Journal

Acta Crystallographica Section FWiley

Published: Nov 1, 2011

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