title: Crystallization and preliminary X-ray analysis of ocr, the product of gene 0.3 of bacteriophage T7.
abstract: Ocr, the product of gene 0.3 of bacteriophage T7, prevents the action of restriction endonucleases of the host bacteria. The amino-acid sequence of ocr has less than 20% similarity to any protein of known three-dimensional structure. Ocr has been crystallized in a number of different crystal forms and X-ray data for the seleno-L-methionine-substituted form has been collected to a resolution of 1.8 A. The presence of caesium was found to be required for good crystal growth. Anomalous X-ray data was used to identify possible positions for Se and Cs atoms in the unit cell.
authors.affiliation: Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh, Scotland.
authors.forename: S S
authors.initials: SS
authors.lastname: Sturrock
authors.forename: D T
authors.initials: DT
authors.lastname: Dryden
authors.forename: C
authors.initials: C
authors.lastname: Atanasiu
authors.forename: J
authors.initials: J
authors.lastname: Dornan
authors.forename: S
authors.initials: S
authors.lastname: Bruce
authors.forename: A
authors.initials: A
authors.lastname: Cronshaw
authors.forename: P
authors.initials: P
authors.lastname: Taylor
authors.forename: M D
authors.initials: MD
authors.lastname: Walkinshaw
mesh_terms: D000595:Amino Acid Sequence; D017123:Bacteriophage T7 / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: C440255:Ocr protein, bacteriophage T7; D014764:Viral Proteins