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

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, w...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-12, Vol.57 (12), p.1776-1785
Hauptverfasser: Terwisscha van Scheltinga, Anke C., Valegård, Karin, Ramaswamy, S., Hajdu, Janos, Andersson, Inger
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container_issue 12
container_start_page 1776
container_title Acta crystallographica. Section D, Biological crystallography.
container_volume 57
creator Terwisscha van Scheltinga, Anke C.
Valegård, Karin
Ramaswamy, S.
Hajdu, Janos
Andersson, Inger
description 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.
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0907-4449
1399-0047
language eng
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source MEDLINE; Crystallography Journals Online; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection
subjects Crystallization
Crystallography, X-Ray
deacetoxycephalosporin C
Intramolecular Transferases - chemistry
merohedral twinning
Models, Molecular
Penicillin-Binding Proteins
Protein Conformation
title Multiple isomorphous replacement on merohedral twins: structure determination of deacetoxycephalosporin C synthase
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