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Structure of Oligomeric β B2-crystallin: an application of the T2 translation function to an asymmetric unit containing two dimers

Driessen, H. P. C., Bax, Benjamin, Slingsby, C., Lindley, P. F., Mahadevan, D., Moss, D. S. and Tickle, I. J. 1991. Structure of Oligomeric β B2-crystallin: an application of the T2 translation function to an asymmetric unit containing two dimers. Acta Crystallographica Section B: Structural Science 47 (6) , pp. 987-997. 10.1107/S0108768191009163

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Abstract

The molecular structure of the main subunit of the fl-crystallins, components of the vertebrate eye lens, has recently been solved by molecular replacement at 2.1 A, resolution [Bax, Lapatto, Nalini, Driessen, Lindley, Mahadevan, Blundell & Slingsby (1990). Nature (London), 347, 776-780]. The protein, fiB2, is a dimer in solution, but a tetramer in the crystal with one subunit in the asymmetric unit of space group 1222. Using the crystallographic dimer from this /-centred form the structure of a C222 crystal form of the fiB2 protein with four subunits in the asymmetric unit has now been solved by molecular replacement at 3.3 A. The solution involved the use of a new translation function for non-crystallographic symmetry, based on the T2 function of Crowther & Blow [Acta Cryst. (1967), 23, 544-548].

Item Type: Article
Status: Published
Schools: Biosciences
Publisher: International Union of Crystallography
ISSN: 0108-7681
Date of Acceptance: 25 July 1991
Last Modified: 16 Jul 2018 15:43
URI: http://orca.cardiff.ac.uk/id/eprint/112654

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