Refinement of macromolecular structures against neutron data with SHELXL2013. (4th February 2014)

• Record Type: Journal Article
• Authors: Gruene, Tim; Hahn, Hinrich W.; Luebben, Anna V.; Meilleur, Flora; Sheldrick, George M.
• Is Part Of: Journal of applied crystallography. Volume 47:Part 1(2014:Feb.)
• Page Start: 462
• Page End: 466
• Publication Date: 2014-02-04
• Subjects: Crystallography -- Periodicals; 548.05
• DOI: 10.1107/S1600576713027659
• Languages: English
• ISSNs: 0021-8898

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Some of the improvements in <italic>SHELX2013</italic> make <italic>SHELXL</italic> 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 <italic>SHELXL</italic> for refinement of protein structures against neutron data. It includes restraints extending the Engh &amp; Huber [<italic>Acta Cryst.</italic> (1991), A<bold>47</bold>, 392–400] restraints to H atoms and discusses several of the features of <italic>SHELXL</italic> that make the program particularly useful for the investigation of H atoms with neutron diffraction. <italic>SHELXL2013</italic> 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.</p> </abstract>