The rise of neutron cryo-crystallography

Hanna Kwon, Patricia S. Langan, Leighton Coates, Emma L. Raven, Peter C.E. Moody

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The use of boiled-off liquid nitrogen to maintain protein crystals at 100 K during X-ray data collection has become almost universal. Applying this to neutron protein crystallography offers the opportunity to significantly broaden the scope of biochemical problems that can be addressed, although care must be taken in assuming that direct extrapolation to room temperature is always valid. Here, the history to date of neutron protein cryo-crystallography and the particular problems and solutions associated with the mounting and cryocooling of the larger crystals needed for neutron crystallography are reviewed. Finally, the outlook for further cryogenic neutron studies using existing and future neutron instrumentation is discussed.

Original languageEnglish
Pages (from-to)792-799
Number of pages8
JournalActa Crystallographica Section D: Structural Biology
Volume74
DOIs
StatePublished - 2018

Funding

The authors wish to acknowledge the support of BBSRC, the Wellcome Trust, ILL and MLZ. Research at the Spallation Neutron Source (SNS) at ORNL was sponsored by the Scientific User Facilities Division, Office of Basic Energy Sciences, US Department of Energy. The Office of Biological and Environmental Research supported research at Oak Ridge National Laboratory’s Center for Structural Molecular Biology (CSMB) using facilities supported by the Scientific User Facilities Division, Office of Basic Energy Sciences, US Department of Energy.

Keywords

  • Cryogenic data collection
  • Enzyme mechanisms
  • Neutron crystallography

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