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Crystallization and Preliminary Crystallographic Analysis of Transgelin

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Abstract:

Transgelin was solubly expressed in E. coli. Crystals of transgelin have been grown at 291K using sodium formate or PEG-4000 as precipitants. X-ray diffraction by the crystal extends to 2.3 Å resolution. The crystal belongs to the space group P21, with the unit cell parameters a=39.3, b=61.9, c=56.0 Å and β =90.2 .





Keywords: Transgelin; crystallization; crystallographic analysis; prokaryotic expression

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607779816122

Affiliations: Capital Medical University,Beijing 100069, People's Republic of China.

Publication date: February 1, 2007

More about this publication?
  • 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.
ben/ppl/2007/00000014/00000002/art00016
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