Structure of oligomeric βB2-crystallin: an application of the T 2 translation function to an asymmetric unit containing two dimers
- 1 December 1991
- journal article
- Published by International Union of Crystallography (IUCr) in Acta crystallographica Section B, Structural science, crystal engineering and materials
- Vol. 47 (6) , 987-997
- https://doi.org/10.1107/s0108768191009163
Abstract
The molecular structure of the main subunit of the beta-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, beta B2, is a dimer in solution, but a tetramer in the crystal with one subunit in the asymmetric unit of space group I222. Using the crystallographic dimer from this I-centred form the structure of a C222 crystal form of the beta B2 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].Keywords
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