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Crystallization and Preliminary X-Ray Studies of the Unliganded Wild-Type Bovine Thrombin

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Wild type of bovine thrombin has been crystallized in a ligand-free form by the hanging drop vapor diffusion method with polyethylene glycol 4000 and 2-propanol. The crystals belong to space group P43212 with unit cell parameters of a = b = 87.7 Å, c = 195.9 Å. X-ray diffraction data were collected to 2.8 Å resolution.

Keywords: Thrombin; blood coagulation system; crystallization

Document Type: Research Article


Publication date: September 1, 2007

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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.

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