Neutron structure determination via macromolecular H/D derivatives

Macromolecular structure phasing by neutron anomalous diffraction

In this report we show for the first time that neutron anomalous dispersion can be used in a practical manner to determine experimental phases of a protein crystal structure, providing a new tool for structural biologists. The approach is demonstrated through the use of a state-of-the-art monochromatic neutron diffractometer at the Institut Laue-Langevin (ILL) in combination with crystals of pe...

A new principle for macromolecular structure determination

Protein NMR spectroscopy is a modern experimental technique for elucidating the threedimensional structure of biological macromolecules in solution. From the data-analytical point of view, structure determination has always been considered an optimisation problem: much effort has been spent on the development of minimisation strategies; the underlying rationale, however, has not been revised. C...

Dipolar couplings in macromolecular structure determination.

Macromolecular structure determination by cryo-electron microscopy.

Recent advances in transmission electron microscopy (EM) hardware, low-temperature methods and image-processing software have made cryo-EM an important complement to X-ray crystallography and NMR for macromolecular structure determination, particularly of large assemblies. This review provides a summary of the main advances and a survey of the capabilities of this approach.

Determination of the neutron spin structure function.

The neutron spin-structure function g 1 has been determined by measuring the asymmetry in deep inelastic scattering of polarized electrons off a polarized He target. The results are interpreted in the quark-parton model and used, in conjuction with earlier proton results, to test the Bjorken sum rule. A measurement of the neutron spin-structure function gn 1 at SLAC by deep inelastic scattering...