Abstract
Human calcyphosine was cloned into the pET-28a vector and highly expressed in Escherichia coli BL21 (DE3) cells. The protein was purified and crystallized. The crystal diffracted to 2.8 Å and belonged to space group P21212, with the unit cell parameters a=70.39 Å, b=132.02 Å, c=46.20 Å.
Protein & Peptide Letters
Title: Crystallization and Preliminary Crystallographic Analysis of Recombinant Human Calcyphosine
Volume: 16 Issue: 3
Author(s): Hui Dong, Zhiyong Lou, Xiaoling Xu, Dan Su, Xiaohong Zhou, Xin Li and Mark Bartlam
Affiliation:
Abstract: Human calcyphosine was cloned into the pET-28a vector and highly expressed in Escherichia coli BL21 (DE3) cells. The protein was purified and crystallized. The crystal diffracted to 2.8 Å and belonged to space group P21212, with the unit cell parameters a=70.39 Å, b=132.02 Å, c=46.20 Å.
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Cite this article as:
Dong Hui, Lou Zhiyong, Xu Xiaoling, Su Dan, Zhou Xiaohong, Li Xin and Bartlam Mark, Crystallization and Preliminary Crystallographic Analysis of Recombinant Human Calcyphosine, Protein & Peptide Letters 2009; 16 (3) . https://dx.doi.org/10.2174/092986609787601624
DOI https://dx.doi.org/10.2174/092986609787601624 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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