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

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

Authors:
 [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)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1261425
Grant/Contract Number:  
AC05-00OR22725; GA-2013-100
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Acta Crystallographica. Section F, Structural Biology Communications
Additional Journal Information:
Journal Volume: 71; Journal Issue: 4; Journal ID: ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY; large-volume crystals; neutron macromolecular crystallography

Citation Formats

Ng, Joseph D., Baird, James K., Coates, Leighton, Garcia-Ruiz, Juan M., Hodge, Teresa A., and Huang, Sijay. Large-volume protein crystal growth for neutron macromolecular crystallography. United States: N. p., 2015. Web. doi:10.1107/S2053230X15005348.
Ng, Joseph D., Baird, James K., Coates, Leighton, Garcia-Ruiz, Juan M., Hodge, Teresa A., & Huang, Sijay. Large-volume protein crystal growth for neutron macromolecular crystallography. United States. doi:10.1107/S2053230X15005348.
Ng, Joseph D., Baird, James K., Coates, Leighton, Garcia-Ruiz, Juan M., Hodge, Teresa A., and Huang, Sijay. Mon . "Large-volume protein crystal growth for neutron macromolecular crystallography". United States. doi:10.1107/S2053230X15005348. https://www.osti.gov/servlets/purl/1261425.
@article{osti_1261425,
title = {Large-volume protein crystal growth for neutron macromolecular crystallography},
author = {Ng, Joseph D. and Baird, James K. and Coates, Leighton and Garcia-Ruiz, Juan M. and Hodge, Teresa A. and Huang, Sijay},
abstractNote = {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.},
doi = {10.1107/S2053230X15005348},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
number = 4,
volume = 71,
place = {United States},
year = {Mon Mar 30 00:00:00 EDT 2015},
month = {Mon Mar 30 00:00:00 EDT 2015}
}

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Free Publicly Available Full Text
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Cited by: 7 works
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