title: Crystallization and preliminary X-ray diffraction studies of a toxic crystal protein from a subspecies of Bacillus thuringiensis.
abstract: The toxic crystal protein (Mr 64,000) from a subspecies of the bacterium Bacillus thuringiensis has been solubilized and recrystallized yielding diffraction quality crystals. Crystals are obtained by a change in pH and ionic strength using Na2CO3. They can also be obtained by a change in ionic strength only using NaBr as the precipitant. The space group of both forms is C222(1) with a = 133, b = 116, c = 104 A and one molecule/asymmetric unit. Still photographs show reflections to 3.0-A resolution.
authors.affiliation: Research Institute of Scripps Clinic, La Jolla, California 92037.
authors.forename: J L
authors.initials: JL
authors.lastname: Garfield
authors.forename: C D
authors.initials: CD
authors.lastname: Stout
mesh_terms: D001413:Bacillus thuringiensis / Q000032:analysis*; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D003460:Crystallization; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009994:Osmolar Concentration; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins