Abstract
The Protein Crystallography Station (PCS), located at the Los Alamos Neutron Scattering Center (LANSCE), was the first macromolecular crystallography beamline to be built at a spallation neutron source. Following testing and commissioning, the PCS user program was funded by the Biology and Environmental Research program of the Department of Energy Office of Science (DOE-OBER) for 13 years (2002-2014). The PCS remained the only dedicated macromolecular neutron crystallography station in North America until the construction and commissioning of the MaNDi and IMAGINE instruments at Oak Ridge National Laboratory, which started in 2012. The instrument produced a number of research and technical outcomes that have contributed to the field, clearly demonstrating the power of neutron crystallo-graphy in helping scientists to understand enzyme reaction mechanisms, hydrogen bonding and visualization of H-atom positions, which are critical to nearly all chemical reactions. During this period, neutron crystallography became a technique that increasingly gained traction, and became more integrated into macromolecular crystallography through software developments led by investigators at the PCS. This review highlights the contributions of the PCS to macromolecular neutron crystallography, and gives an overview of the history of neutron crystallography and the development of macromolecular neutron crystallography from the 1960s to the 1990s and onwards through the 2000s.
Highlights
The Protein Crystallography Station (PCS), located at the Los Alamos Neutron Scattering Center (LANSCE), was the first macromolecular crystallography beamline to be built at a spallation neutron source
The instrument produced a number of research and technical outcomes that have contributed to the field, clearly demonstrating the power of neutron crystallography in helping scientists to understand enzyme reaction mechanisms, hydrogen bonding and visualization of H-atom positions, which are critical to most chemical reactions
Work was conducted during the early 1990s; Wlodawer, Kossiakoff and others used neutron crys- advances in molecular biology and automation revolutionized tallography to study the dynamics of proteins in a crystalline macromolecular X-ray crystallography during this decade and environment, taking advantage of the different scattering led to a resurgence of interest in neutron crystallography
Summary
One-half of all atoms in a macromolecule are H atoms, and these H atoms play essential roles in macromolecular structure and catalysis. Work was conducted during the early 1990s; Wlodawer, Kossiakoff and others used neutron crys- advances in molecular biology and automation revolutionized tallography to study the dynamics of proteins in a crystalline macromolecular X-ray crystallography during this decade and environment, taking advantage of the different scattering led to a resurgence of interest in neutron crystallography. Becoming increasingly streamlined through hardware (synchrotrons, fast-readout CCD detectors, robotics, cryocooling), software (integrated crystallographic refinement programs) and accessible crystallization (high-throughput screening, ready-made crystallization screening kits) These developments opened up a wide range of proteins for structural biology studies, and helped drive a new demand for neutron diffraction instruments and more efficient data collection. Macromolecular neutron crystallography occupies a very special place in structural molecular science
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