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Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):358-70. doi: 10.1107/S2053230X15005348. Epub 2015 Mar 30.

Large-volume protein crystal growth for neutron macromolecular crystallography.

Author information

1
Department of Biological Sciences, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
2
Department of Chemistry, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
3
Biology and Soft Matter Division, Oak Ridge National Laboratory, PO Box 2008, MS6475, Oak Ridge, TN 37831, USA.
4
Laboratorio de Estudios Cristalográficos (IACT), CSIC-Universidad de Granada, Avenida de la Innovación s/n, Armilla (Granada), Spain.

Abstract

Neutron macromolecular crystallography (NMC) is the prevailing method for the accurate determination of the positions of H atoms in macromolecules. As neutron sources are becoming more available to general users, finding means to optimize the growth of protein crystals to sizes suitable for NMC is extremely important. Historically, much has been learned about growing crystals for X-ray diffraction. However, owing to new-generation synchrotron X-ray facilities and sensitive detectors, protein crystal sizes as small as in the nano-range have become adequate for structure determination, lessening the necessity to grow large crystals. Here, some of the approaches, techniques and considerations for the growth of crystals to significant dimensions that are now relevant to NMC are revisited. These include experimental strategies utilizing solubility diagrams, ripening effects, classical crystallization techniques, microgravity and theoretical considerations.

KEYWORDS:

large-volume crystals; neutron macromolecular crystallography

PMID:
25849493
PMCID:
PMC4388167
DOI:
10.1107/S2053230X15005348
[Indexed for MEDLINE]
Free PMC Article

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