High resolution neutron crystallographic studies of the dynamical phase transition in perdeuterated rubredoxin
We request beamtime on D19 for a multi cryo temperature (175 K, 200 K and 240 K) crystallographic study of perdeuterated rubredoxin, a never-done-before neutron data collection using a new crystallographic approach in order to shed light on the microscopic conundrum of the protein dynamical transition. This proposal is an opportunity to analyse the dynamical transition in protein by completing the high quality and unique results obtained from D19 experiments 1-20-16 and 1-20-18. It provided crystallographic data with high completeness at 295 K (article submitted for publication) and 100 K (data analysis and preparation for publication in progress) to atomic resolutions of 1.27 Å and 0.90 Å, respectively. The neutron study shall be complemented by the high resolution synchrotron X-ray crystallographic results (expected to better than 1.00 Å resolution) at the same three temperatures for better completeness of the study. The perdeuterated rubredoxin crystals suitable for the neutron experiment are already available and have proven to be highly resistant to extremely low temperature conditions, making it ideal for the study.
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CUYPERS Maxime; FORSYTH Victor Trevor; MASON, Sax A.; MITCHELL Edward; MOSSOU Estelle and ZACCAI Joseph. (2013). High resolution neutron crystallographic studies of the dynamical phase transition in perdeuterated rubredoxin. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-402
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