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Multiple isomorphous replacement on merohedral twins: structure determination of deacetoxycephalosporin C synthase

By Anke C. Terwisscha van Scheltinga, Karin Valegård, S. Ramaswamy, Janos Hajdu and Inger Andersson

Abstract

Merohedral twinning is a packing anomaly that seriously impairs the determination of macromolecular crystal structures. Crystals of deacetoxycephalosporin C synthase (DAOCS), an enzyme involved in the expansion of the penicillin nucleus to form the core structure of the cephalosporin antibiotics, were found to be merohedrally twinned by many diagnostic criteria. Here, the structure determination of DAOCS from twinned crystals based on a combination of isomorphous replacement and the use of a multiple-wavelength diffraction data set is described.

Year: 2001
DOI identifier: 10.1107/s0907444901014081
OAI identifier: oai:ub.rug.nl:dbi/4a2d147bd7c94
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