Open AccessAnomalies in the refinement of isoleucine
Author(s) -
Berntsen Karen R. M.,
Vriend Gert
Publication year - 2014
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s139900471400087x
Subject(s) - torsion (gastropod) , software , computer science , low resolution , conformational isomerism , crystallography , high resolution , algorithm , computational science , physics , chemistry , molecule , biology , programming language , geology , zoology , remote sensing , quantum mechanics
A study of isoleucines in protein structures solved using X‐ray crystallography revealed a series of systematic trends for the two side‐chain torsion angles χ 1 and χ 2 dependent on the resolution, secondary structure and refinement software used. The average torsion angles for the nine rotamers were similar in high‐resolution structures solved using either the REFMAC , CNS or PHENIX software. However, at low resolution these programs often refine towards somewhat different χ 1 and χ 2 values. Small systematic differences can be observed between refinement software that uses molecular dynamics‐type energy terms (for example CNS ) and software that does not use these terms (for example REFMAC ). Detailing the standard torsion angles used in refinement software can improve the refinement of protein structures. The target values in the molecular dynamics‐type energy functions can also be improved.