Crystallization and preliminary X-ray investigation of the complex of RNase Sa with wild-type barstar
| Autor: | Lubica Urbanikova, Jozef Sevcik |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Barnase
biology Bacillus amyloliquefaciens RNase P Streptomyces aureofaciens General Medicine biology.organism_classification Crystallography X-Ray Isoenzymes chemistry.chemical_compound Crystallography Ribonucleases chemistry Bacterial Proteins Structural Biology biology.protein Ribonuclease Barstar Sodium dodecyl sulfate Enzyme Inhibitors Polyacrylamide gel electrophoresis |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 54(Pt 3) |
| ISSN: | 0907-4449 |
| Popis: | RNase Sa, an extracellular ribonuclease produced by Streptomyces aureofaciens, is inhibited by barstar, the natural protein inhibitor of barnase, the ribonuclease of Bacillus amyloliquefaciens. The complex of RNase Sa with wild-type barstar was crystallized by hanging-drop vapour diffusion. It was shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis that RNase Sa and barstar are present in equimolar proportions in the crystals. The crystals are in the hexagonal space group P65 with unit cell dimensions a = b = 56.95, c = 135.8 Å. They diffract to 1.7 Å resolution at the DESY synchronton source. The asymmetric unit contains one molecule of the complex. |
| Databáze: | OpenAIRE |
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