Publication Date:
2012-01-25
Description:
Bacteriophage T7 attaches to its host using the C-terminal domains of its six fibres, which are trimers of the gp17 protein. A C-terminal fragment of gp17 consisting of amino acids 371–553 has been expressed, purified and crystallized. Crystals of two forms were obtained, belonging to space groupP212121(unit-cell parametersa= 61.2,b= 86.0,c= 118.4 Å) and space groupC2221(unit-cell parametersa= 68.3,b= 145.6,c= 172.1 Å). They diffracted to 1.9 and 2.0 Å resolution, respectively. Both crystals are expected to contain one trimer in the asymmetric unit. Multiwavelength anomalous dispersion phasing with a mercury derivative is in progress.
Print ISSN:
1744-3091
Topics:
Biology
,
Chemistry and Pharmacology
,
Geosciences
,
Physics
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