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Crystallization and prelilminary X‐ray investigation of barster, the intracellular inhibitor of barnase
Author(s) -
Guillet Valérie,
Lapthorn Adrian,
Fourniat Jacky,
Benoit JeanPierre,
Hartley Robert W.,
Mauguen Yves
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340170309
Subject(s) - barnase , crystallography , crystallization , chemistry , superstructure , crystal structure , molecule , resolution (logic) , bacillus amyloliquefaciens , crystal (programming language) , ribonuclease , physics , organic chemistry , thermodynamics , rna , biochemistry , artificial intelligence , computer science , fermentation , programming language , gene
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.