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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