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Detalle de: Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17

Title Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17
Abstract

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 group P 2 1 2 1 2 1 (unit-cell parameters a = 61.2, b = 86.0, c = 118.4 Å) and space group C 222 1 (unit-cell parameters a = 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.

Apa Reference Garcia-Doval, C. & van Raaij, M.J. (2012). Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(2), 166-171. 10.1107/S1744309111051049
Doi 10.1107/S1744309111051049
Publication Date 25 Jan 2012
Publication Type Article
Researcher Mark van Raaij
Ontology Viromics
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