Your browser doesn't support javascript.
loading
Crystallization and preliminary X-ray analysis of ocr, the product of gene 0.3 of bacteriophage T7.
Sturrock, S S; Dryden, D T; Atanasiu, C; Dornan, J; Bruce, S; Cronshaw, A; Taylor, P; Walkinshaw, M D.
Affiliation
  • Sturrock SS; Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh, Scotland.
Acta Crystallogr D Biol Crystallogr ; 57(Pt 11): 1652-4, 2001 Nov.
Article in En | MEDLINE | ID: mdl-11679734
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.
Subject(s)
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Viral Proteins / Bacteriophage T7 Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 2001 Document type: Article Affiliation country: Reino Unido
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Viral Proteins / Bacteriophage T7 Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 2001 Document type: Article Affiliation country: Reino Unido
...