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Title: Large-volume protein crystal growth for neutron macromolecular crystallography

Journal Article · · Acta Crystallographica. Section F, Structural Biology Communications
 [1];  [2];  [3];  [4];  [2];  [2]
  1. Univ. of Alabama in Huntsville,, Huntsville, AL (United States). Dept. of Biological Sciences; iXpressGenes Inc.,Huntsville, AL (United States). Hudson Alpha Inst. for Biotechnology
  2. Univ. of Alabama in Huntsville,, Huntsville, AL (United States). Dept. of Chemistry
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Biology and Soft matter Division
  4. Univ. of Granada (Spain). Lab. of Crystallographic Studies (IACT)

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. We report that these include experimental strategies utilizing solubility diagrams, ripening effects, classical crystallization techniques, microgravity and theoretical considerations.

Research Organization:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-00OR22725; GA-2013-100
OSTI ID:
1261425
Journal Information:
Acta Crystallographica. Section F, Structural Biology Communications, Vol. 71, Issue 4; ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English

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  • Acta Crystallographica Section F Structural Biology and Crystallization Communications, Vol. 68, Issue 12 https://doi.org/10.1107/S1744309112032447
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