title: Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre.
abstract: Tails of bacteriophage T5 (a member of the Siphoviridae family) were studied by electron microscopy. For the distal parts of the L-shaped tail fibres, which are involved in host cell receptor binding, a low-resolution volume was calculated. Several C-terminal fragments of the fibre were expressed and purified. Crystals of two of them were obtained that belonged to space groups P63 and R32 and diffracted synchrotron radiation to 2.3 and 2.9 Å resolution, respectively. A single-wavelength anomalous dispersion data set to 2.5 Å resolution was also collected from a selenomethionine-derivatized crystal of one of the fragments, which belonged to space group C2.
authors: Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Calle Darwin 3, 28049 Madrid, Spain.
authors: Carmela
authors: C
authors: Garcia-Doval
authors: Daniel
authors: D
authors: Luque
authors: José R
authors: JR
authors: Castón
authors: Pascale
authors: P
authors: Boulanger
authors: Mark J
authors: MJ
authors: van Raaij
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D058645:Denaturing Gradient Gel Electrophoresis; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D008854:Microscopy, Electron; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017906:Siphoviridae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017356:Synchrotrons; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D017376:Viral Tail Proteins
keywords: Siphoviridae; bacteriophage T5