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Crystals 2017, 7(10), 296; doi:10.3390/cryst7100296

Over-Production, Crystallization, and Preliminary X-ray Crystallographic Analysis of a Coiled-Coil Region in Human Pericentrin

School of Systems Biomedical Science, Soongsil University, Seoul 06978, Korea
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Academic Editor: Jolanta Prywer
Received: 12 September 2017 / Revised: 27 September 2017 / Accepted: 28 September 2017 / Published: 2 October 2017
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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Abstract

The genes encoding three coiled-coil regions in human pericentrin were gene synthesized with Escherichia coli codon-optimization, and the proteins were successfully over-produced in large quantities using E. coli expression. After verifying that the purified proteins were mostly composed of α-helices, one of the proteins was crystallized using polyethylene glycol 8000 as crystallizing agent. X-ray diffraction data were collected to 3.8 Å resolution under cryo-condition using synchrotron X-ray. The crystal belonged to space group C2 with unit cell parameters a = 324.9 Å, b = 35.7 Å, c = 79.5 Å, and β = 101.6˚. According to Matthews’ coefficient, the asymmetric unit may contain up to 12 subunits of the monomeric protein, with a crystal volume per protein mass (VM) of 1.96 Å3 Da−1 and a 37.3% solvent content. View Full-Text
Keywords: pericentrin; coiled-coil; centrosome; pericentriolar material (PCM) pericentrin; coiled-coil; centrosome; pericentriolar material (PCM)
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Kim, M.Y.; Park, J.K.; Sim, Y.; Kim, D.; Sim, J.Y.; Park, S. Over-Production, Crystallization, and Preliminary X-ray Crystallographic Analysis of a Coiled-Coil Region in Human Pericentrin. Crystals 2017, 7, 296.

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