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 ORCID: https://orcid.org/0000-0003-1940-3785, 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:	23 Oct 2022 14:03
URI:	https://orca.cardiff.ac.uk/id/eprint/112654

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