Crystallization of the C‐terminal domain of the bacteriophage T5 L‐shaped fibre. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Garcia‐Doval, Carmela; Luque, Daniel; Castón, José R.; Boulanger, Pascale; van Raaij, Mark J.
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1363
• Page End: 1367
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113028959
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Tails of bacteriophage T5 (a member of the <italic>Siphoviridae</italic> 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 <italic>P</italic>6₃ and <italic>R</italic>32 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 <italic>C</italic>2.</p> </abstract>