Large-volume protein crystal growth for neutron macromolecular crystallography

Joseph D. Ng, James K. Baird, Leighton Coates, Juan M. Garcia-Ruiz, Teresa A. Hodge, Sijay Huang

    Research output: Contribution to journalArticlepeer-review

    31 Scopus citations

    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.

    Original languageEnglish
    Pages (from-to)358-370
    Number of pages13
    JournalActa Crystallographica Section F:Structural Biology Communications
    Volume71
    DOIs
    StatePublished - Apr 1 2015

    Keywords

    • large-volume crystals
    • neutron macromolecular crystallography

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