Homology-based hydrogen bond information improves crystallographic structures in the PDB

Author:

van Beusekom Bart1,Touw Wouter G.1,Tatineni Mahidhar2,Somani Sandeep3,Rajagopal Gunaretnam3,Luo Jinquan4,Gilliland Gary L.4,Perrakis Anastassis1ORCID,Joosten Robbie P.1ORCID

Affiliation:

1. Department of Biochemistry; Netherlands Cancer Institute, Plesmanlaan 121; Amsterdam 1066 CX The Netherlands

2. San Diego Supercomputer Center, University of California, San Diego, 9500 Gilman Drive; La Jolla California 92093-0505

3. Discovery Sciences, Janssen R&D LLC; Spring House Pennsylvania

4. Janssen BioTherapeutics, Janssen R&D LLC; Spring House Pennsylvania

Funder

Netherlands Organisation for Scientific Research

Horizon 2020 Framework Programme

iNEXT

Johnson and Johnson

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference37 articles.

1. Homo crystallographicus - quo vadis?;Kleywegt;Structure,2002

2. Accurate bond and angle parameters for X-ray protein structure refinement;Engh;Acta Cryst,1991

3. New parameters for the refinement of nucleic acid-containing structures;Parkinson;Acta Cryst,1996

4. Conditional restraints”: restraining the free atoms in ARP/wARP;Mooij;Structure,2009

5. Use of knowledge-based restraints in phenix.refine to improve macromolecular refinement at low resolution;Headd;Acta Cryst,2012

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