Crystallization and preliminary X-ray analysis of ocr, the product of gene 0.3 of bacteriophage T7

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 57; no. 11; pp. 1652 - 1654
• Main Authors: Sturrock, Shane S., Dryden, David T. F., Atanasiu, Constandache, Dornan, Jacqueline, Bruce, Sandra, Cronshaw, Andrew, Taylor, Paul, Walkinshaw, Malcolm D.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.11.2001
• Subjects: Amino Acid Sequence; anti-restriction; bacteriophage; Bacteriophage T7 - chemistry; Crystallization; Crystallography, X-Ray; gene 0.3; Molecular Sequence Data; ocr; Protein Conformation; Viral Proteins - chemistry
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444901011623

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 Å. 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.