Crystallization and Preliminary Crystallographic Analysis of Recombinant Human Calcyphosine

Authors: Dong, Hui; Lou, Zhiyong; Xu, Xiaoling; Su, Dan; Zhou, Xiaohong; Li, Xin; Bartlam, Mark

Source: Protein and Peptide Letters, Volume 16, Number 3, March 2009 , pp. 339-341(3)

Publisher: Bentham Science Publishers

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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.

Document Type: Research article

DOI: http://dx.doi.org/10.2174/092986609787601624

Publication date: 2009-03-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.