Journal ArticleDOI
Rapid visualization of hydrogen positions in protein neutron crystallographic structures
Parthapratim Munshi,Parthapratim Munshi,Shang-Lin Chung,Matthew P. Blakeley,Kevin L. Weiss,Dean A. A. Myles,Flora Meilleur,Flora Meilleur +7 more
TLDR
Comparison of perdeuterated rubredoxin structures refined against neutron data sets collected over hours and up to 5 d shows that rapid neutron data collection in just 14 h is sufficient to provide the positions of 269 D atoms without ambiguity.Abstract:
Neutron crystallography is a powerful technique for experimental visualization of the positions of light atoms, including hydrogen and its isotope deuterium. In recent years, structural biologists have shown increasing interest in the technique as it uniquely complements X-ray crystallographic data by revealing the positions of D atoms in macromolecules. With this regained interest, access to macromolecular neutron crystallography beamlines is becoming a limiting step. In this report, it is shown that a rapid data-collection strategy can be a valuable alternative to longer data-collection times in appropriate cases. Comparison of perdeuterated rubredoxin structures refined against neutron data sets collected over hours and up to 5 d shows that rapid neutron data collection in just 14 h is sufficient to provide the positions of 269 D atoms without ambiguity.read more
Citations
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Journal ArticleDOI
An Overview of Biological Macromolecule Crystallization
TL;DR: The general aspects of protein crystallization are introduced, conventional and innovative crystallization methods are summarized and the new strategies utilized to improve the success rate of experiments and increase crystal diffraction quality are focused on.
Journal ArticleDOI
Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential
TL;DR: Neutron crystallography and sub-atomic X-ray crystallography complement each other in defining hydrogen positions in macromolecules and much effort is still required to become a mainstream activity.
Journal ArticleDOI
The Bio‐SANS instrument at the High Flux Isotope Reactor of Oak Ridge National Laboratory
William T. Heller,Volker S. Urban,Gary W. Lynn,Kevin L. Weiss,Hugh O'Neill,Sai Venkatesh Pingali,Shuo Qian,Kenneth C. Littrell,Yuri B. Melnichenko,Michelle V. Buchanan,Douglas L Selby,George D. Wignall,Paul Butler,Dean A. A. Myles +13 more
TL;DR: The Bio-SANS instrument of the High Flux Isotope Reactor of Oak Ridge National Laboratory (ORNL) is a high-flux low-background SANS instrument that is, uniquely among SANS instruments, dedicated to serving the needs of the structural biology and biomaterials communities as an open-access user facility as discussed by the authors.
Journal ArticleDOI
Neutron protein crystallography: A complementary tool for locating hydrogens in proteins
TL;DR: Methods to produce isotopically-substituted proteins and to grow large crystals are provided in the context of neutron structures reported in the literature along with technique-specific strategies including joint X-ray/neutron structure refinement.
Journal ArticleDOI
The IMAGINE instrument: first neutron protein structure and new capabilities for neutron macromolecular crystallography.
Flora Meilleur,Parthapratim Munshi,Lee Robertson,Alexandru D. Stoica,Lowell Crow,Andrey Kovalevsky,Tibor S Koritsanszky,Bryan C. Chakoumakos,Robert H. Blessing,Dean A. A. Myles +9 more
TL;DR: The first high-resolution neutron protein structure of perdeuterated rubredoxin from Pyrococcus furiosus (PfRd) determined using the new IMAGINE macromolecular neutron crystallography instrument at the Oak Ridge National Laboratory is reported.
References
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