posted on 2018-08-14, 14:17authored byHanna Kwon, Patricia Langan, Leighton Coates, Emma Raven, Peter Moody
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 we review 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. Finally, we discuss the
outlook for further cryogenic neutron studies using existing and future neutron
instrumentation.
Funding
The authors wish to acknowledge the contributions of Matthew Blakeley, Cecilia Casadei,
Andreas Ostermann, and Tobias Schrader and the support of BBSRC, Wellcome Trust, ILL,
MLZ and the Laboratory Directed Research and Development Program of Oak Ridge
National Laboratory (ORNL), managed by UT-Battelle LLC for the US Department of
Energy under contract No. DE-AC05- 00OR22725. 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.