Crystallization and preliminary X-ray investigation of the complex of RNase Sa with wild-type barstar

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 54; no. 3; pp. 403 - 404
• Main Authors: Urbanikova, Lubica, Sevcik, Jozef
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.05.1998
• Subjects: Bacterial Proteins - pharmacology; Crystallography, X-Ray; Enzyme Inhibitors - pharmacology; Isoenzymes - antagonists & inhibitors; Ribonucleases - antagonists & inhibitors; Streptomyces aureofaciens - enzymology
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444997010688

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 ab 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.