Corrigendum to “Semi-Rigid Solution Structures of Heparin by Constrained X-ray Scattering Modelling: New Insight into Heparin–Protein Complexes” [J. Mol. Biol. 395 (2010) 504–521]
Sanaullah Khan1, Jayesh Gor1, Barbara Mulloy2 and Stephen J. Perkins1 1 - Department of Structural and Molecular Biology, Division of Biosciences, Darwin Building, University College London, Gower Street, London WC1E 6BT, UK 2 - National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, UK
Correspondence to Stephen J. Perkins: [email protected]
DOI of the original article: http://dx.doi.org/10.1016/j.jmb.2009.10.064 http://dx.doi.org/10.1016/j.jmb.2013.02.028
The four heparin oligosaccharide structures dp18–dp36 reported in the original paper contained poor intramolecular contacts. A constant force field termed DREIDING minimization provided in Discovery Studio (Accelrys) was used to correct this. These corrected heparin structures have been used in two recent studies [Khan et al. (2011). J. Biol. Chem. 286, 24842–24854; Khan et al. (2012). Biochem. J. 444, 417–428]. The newly refined structures have been deposited in the Protein Data Bank with accession codes 4J8H (dp18), 4J8I (dp24), 4J8J (dp30), and 4J8K (dp36). See Supplementary Material. The corrected structures confirm that heparin remains semi-rigid and extended in appearance and the conclusions of the original paper remain valid. Supplementary data to this article can be found online at http://dx.doi.org/10.1016/j.jmb.2013.02.028
0022-2836/$ - see front matter © 2013 Elsevier Ltd. All rights reserved.
J. Mol. Biol. (2013) 425, 1847