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J Appl Crystallogr. 2013 Dec 7;47(Pt 1):462-466. eCollection 2014 Feb 1.

Refinement of macromolecular structures against neutron data with SHELXL2013.

Author information

1
Department of Structural Chemistry, Georg-August-University Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany.
2
North Carolina State University, Raleigh, NC 27695, USA ; Oak Ridge National Laboratory, Oak Ridge, TN 37831-6142, USA.

Abstract

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), A47, 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.

KEYWORDS:

SHELXL2013; hydrogen restraints; macromolecular structure refinement; single-crystal neutron diffraction

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