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Refinement of macromolecular structures against neutron data with SHELXL2013
Author(s) -
Gruene Tim,
Hahn Hinrich W.,
Luebben Anna V.,
Meilleur Flora,
Sheldrick George M.
Publication year - 2014
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s1600576713027659
Subject(s) - neutron , neutron diffraction , macromolecule , computer science , protocol (science) , crystallography , chemistry , physics , nuclear physics , crystal structure , medicine , biochemistry , alternative medicine , pathology
Some of the improvements in SHELX2013 make SHELXL convenient to use for refinement of macromolecular structures against neutron data without the support of X‐ray data. The new NEUT instruction adjusts the behaviour of the SFAC instruction as well as the default bond lengths of the AFIX instructions. This work presents a protocol on how to use SHELXL for refinement of protein structures against neutron data. It includes restraints extending the Engh & Huber [ Acta Cryst. (1991), A 47 , 392–400] restraints to H atoms and discusses several of the features of SHELXL that make the program particularly useful for the investigation of H atoms with neutron diffraction. SHELXL2013 is already adequate for the refinement of small molecules against neutron data, but there is still room for improvement, like the introduction of chain IDs for the refinement of macromolecular structures.