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Crystals 2017, 7(10), 296;

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
Author to whom correspondence should be addressed.
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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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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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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