Crystallization and preliminary X-ray diffraction data of the complex of recombinant tick anticoagulant peptide (rTAP) and bovine factor Xa
| Autor: | Richard S. Alexander, Stuart A. Rosenfeld, Anzhi Wei, Chong-Hwan Chang, Harold D. Ross, Angela Smallwood, J. L. Duke |
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| Rok vydání: | 1999 |
| Předmět: |
medicine.drug_mechanism_of_action
Stereochemistry Factor Xa Inhibitor Polyethylene glycol Crystallography X-Ray Arthropod Proteins law.invention chemistry.chemical_compound Ticks Structural Biology law medicine Animals Crystallization Resolution (electron density) General Medicine Recombinant Proteins Crystallography chemistry Factor Xa X-ray crystallography Recombinant DNA Intercellular Signaling Peptides and Proteins Cattle Electrophoresis Polyacrylamide Gel Peptides Tick anticoagulant peptide Factor Xa Inhibitors |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 55:862-864 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444998017673 |
| Popis: | The complex of bovine factor Xa and recombinant tick anticoagulant peptide (rTAP) was crystallized in two different crystal forms using polyethylene glycol as a precipitant. Form I belongs to space group P42212 with unit-cell dimensions a = b = 133.1, c = 68.8 Å. It contains one complex per asymmetric unit and diffracts to 3.0 Å resolution. Form II belongs to P41212 (or P43212) with dimensions a = b = 126.5, c = 146.7 Å; it contains two complexes per asymmetric unit and diffracts to 2.5 Å. The crystals of both forms consist of factor Xa (MW = 45.3 kDa) and rTAP (MW = 6.7 kDa). |
| Databáze: | OpenAIRE |
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