The University of Southampton
University of Southampton Institutional Repository
Warning ePrints Soton is experiencing an issue with some file downloads not being available. We are working hard to fix this. Please bear with us.

Structural analysis of glycoproteins: building N-linked glycans with Coot

Structural analysis of glycoproteins: building N-linked glycans with Coot
Structural analysis of glycoproteins: building N-linked glycans with Coot
Coot is a graphics application that is used to build or manipulate macromolecular
models; its particular forte is manipulation of the model at the residue level. The
model-building tools of Coot have been combined and extended to assist or
automate the building of N-linked glycans. The model is built by the addition of
monosaccharides, placed by variation of internal coordinates. The subsequent
model is refined by real-space refinement, which is stabilized with modified and
additional restraints. It is hoped that these enhanced building tools will help to
reduce building errors of N-linked glycans and improve our knowledge of the
structures of glycoproteins.
0907-4449
Emsley, Paul
4eaa0012-7fa6-43e7-82a1-0049231a8d1f
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Emsley, Paul
4eaa0012-7fa6-43e7-82a1-0049231a8d1f
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

Emsley, Paul and Crispin, Max (2018) Structural analysis of glycoproteins: building N-linked glycans with Coot. Acta Crystallographica Section D: Biological Crystallography, 74 (4). (doi:10.1107/S2059798318005119).

Record type: Article

Abstract

Coot is a graphics application that is used to build or manipulate macromolecular
models; its particular forte is manipulation of the model at the residue level. The
model-building tools of Coot have been combined and extended to assist or
automate the building of N-linked glycans. The model is built by the addition of
monosaccharides, placed by variation of internal coordinates. The subsequent
model is refined by real-space refinement, which is stabilized with modified and
additional restraints. It is hoped that these enhanced building tools will help to
reduce building errors of N-linked glycans and improve our knowledge of the
structures of glycoproteins.

Text
ba5284 - Version of Record
Available under License Creative Commons Attribution.
Download (936kB)

More information

Accepted/In Press date: 29 March 2018
e-pub ahead of print date: 6 April 2018
Published date: April 2018

Identifiers

Local EPrints ID: 419834
URI: http://eprints.soton.ac.uk/id/eprint/419834
ISSN: 0907-4449
PURE UUID: 10df4a32-c788-44d9-9be0-89aa975a4b1d
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 23 Apr 2018 16:30
Last modified: 26 Nov 2021 03:11

Export record

Altmetrics

Contributors

Author: Paul Emsley
Author: Max Crispin ORCID iD

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×