Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17.
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 P2(1)2(1)2(1) (unit-cell parameters a = 61.2, b = 86.0, c = 118.4 Å) and space group C222(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.
Departamento de Estructuras de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), Madrid, Spain.
Carmela
C
Garcia-Doval
Mark J
MJ
van Raaij
D000595:Amino Acid Sequence; D017123:Bacteriophage T7 / Q000737:chemistry*; D003460:Crystallization; D008969:Molecular Sequence Data; D014764:Viral Proteins / Q000737:chemistry*
D014764:Viral Proteins; C069680:bacteriophage T7 leg protein gp17