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Title: Crystal structure of human CRMP-4: correction of intensities for lattice-translocation disorder

Crystals of human CRMP-4 showed severe lattice-translocation disorder. Intensities were demodulated using the so-called lattice-alignment method and a new more general method with simplified parameterization, and the structure is presented. Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins that are mainly involved in neuronal cell development. In humans, the CRMP family comprises five members. Here, crystal structures of human CRMP-4 in a truncated and a full-length version are presented. The latter was determined from two types of crystals, which were either twinned or partially disordered. The crystal disorder was coupled with translational NCS in ordered domains and manifested itself with a rather sophisticated modulation of intensities. The data were demodulated using either the two-lattice treatment of lattice-translocation effects or a novel method in which demodulation was achieved by independent scaling of several groups of intensities. This iterative protocol does not rely on any particular parameterization of the modulation coefficients, but uses the current refined structure as a reference. The best results in terms of R factors and map correlation coefficients were obtained using this new method. The determined structures of CRMP-4 are similar to those of other CRMPs. Structural comparison allowed the confirmation of known residues, as well as themore » identification of new residues, that are important for the homo- and hetero-oligomerization of these proteins, which are critical to nerve-cell development. The structures provide further insight into the effects of medically relevant mutations of the DPYSL-3 gene encoding CRMP-4 and the putative enzymatic activities of CRMPs.« less
Authors:
 [1] ;  [2] ;  [3] ;  [4] ;  [5]
  1. Universidade Nova de Lisboa, Avenida da República, EAN, 2781-901 Oeiras (Portugal)
  2. Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot OX11 0FA (United Kingdom)
  3. University of Hamburg, Ohnhorststrasse 18, 22609 Hamburg (Germany)
  4. Karolinska Institutet, Tomtebodavägen 6, 4tr, 17177 Stockholm (Sweden)
  5. (Portugal)
Publication Date:
OSTI Identifier:
22347766
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 70; Journal Issue: Pt 6; Other Information: PMCID: PMC4051505; PMID: 24914979; PUBLISHER-ID: dz5326; OAI: oai:pubmedcentral.nih.gov:4051505; Copyright (c) Ponnusamy et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ALIGNMENT; CORRECTIONS; CORRELATIONS; CRYSTAL STRUCTURE; CRYSTALS; CURRENTS; LENGTH; MODULATION; R FACTORS; SCALING; TRANSLOCATION