Crystallization of an enzyme-inhibitor complex: proteinase K with its protein inhibitor, PK13
| Autor: | Demetrius Tsernoglou, Gour P. Pal, Klaus D. Jany |
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| Rok vydání: | 1994 |
| Předmět: |
Ammonium sulfate
Stereochemistry Crystal structure Crystallography X-Ray Biochemistry law.invention chemistry.chemical_compound Structural Biology law Protease Inhibitors Crystallization Molecular Biology biology Molecular mass Serine Endopeptidases Fungi Proteinase K Solvent Crystallography chemistry Enzyme inhibitor biology.protein Chromatography Gel Orthorhombic crystal system Electrophoresis Polyacrylamide Gel Endopeptidase K |
| Zdroj: | Proteins. 19(2) |
| ISSN: | 0887-3585 |
| Popis: | Crystals of a complex of proteinase K (molecular mass, 28,790 Da) with its naturally occurring protein inhibitor PK13 (19,641 Da), have been prepared by a microdialysis technique and modified by hanging drop vapor diffusion against 25% ammonium sulfate in 50 mM Tris-HCl, pH 7.8. The crystals are long prisms with diamond-shaped cross sections of 0.2 × 0.4 × 1.5 mm3 and they diffract X-rays to a resolution of 2.5 A. They belong to the orthorhombic space group P212121 with cell dimensions a = 64.1 A, b = 66.8 A, and c = 133.8 A. Assuming one whole complex in the asymmetric unit, one obtains VM = 2.95 A3/Da and the solvent content, Vsolv = 58.3%. © 1994 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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