Open AccessCrystallization of the C‐terminal domain of the bacteriophage T7 fibre protein gp17
Author(s) -
GarciaDoval Carmela,
van Raaij Mark J.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111051049
Subject(s) - trimer , crystallization , crystallography , bacteriophage , resolution (logic) , substructure , c terminus , chemistry , amino acid , materials science , stereochemistry , dimer , biochemistry , organic chemistry , escherichia coli , artificial intelligence , computer science , gene , structural engineering , engineering
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.