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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 17 (1993), S. 325-328 
    ISSN: 0887-3585
    Keywords: crystallization ; ribonuclease ; inhibitor ; amyloliquefaciens ; protein-protein complex ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Crystals of barstar, the intracellular inhibitor of the extracellular ribonuclease produced by Bacillus amyloliquefaciens (barnase), were obtained through vapor phase equilibration using the hanging drop technique. Three crystal forms have been characterized. Forms I and II, crystallized eithr in potetragonal; they exhibit a superstructure along the c-axis. Form III crystals, suitable for a high resolution structure determination, were grown from 55-65% ammomnium sulfate. This crystal form is hexagonal and diffracts to at least 2 Å resolution at a synchrotron radiation source. It belongs to the hexagonal space group P6, with unit cell dimensions a = b = 143.6 Å, c = 35.6 Å. There are four molecules of barstar in the asymmetric unit. X-ray data have been collected to 2.2 Å Bragg sapcing. The structure determination is underway in order to analyze conformational changes of barstar upon complexation with barnas. © 1993 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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