A study of in vitro refolding and isotope effects on protein structure, activity and stability shows that different folding dynamics can lead to important changes in protein properties.

The Protein Crystallography Station user facility at Los Alamos National Laboratory not only offers open access to a high-performance neutron beamline, but also actively supports and develops new methods in protein expression, deuteration, purification, robotic crystallization and the synthesis of substrates with stable isotopes and provides assistance with data-reduction and structure-refinement software and comprehensive neutron structure analysis.

The capabilities of the Protein Crystallography Station at Los Alamos Neutron Science Center for determining protein structures by spallation neutron crystallography are illustrated, and the methodological and technological advances that are emerging from the Macromolecular Neutron Crystallography consortium are described.

This article highlights scientific and technical contributions from the Protein Crystallography Station at Los Alamos, the first purpose-built macromolecular crystallography station at a spallation neutron source.

The advantages of perdeuteration with regard to solvent visibility in macromolecules is demonstrated through the comparison of two neutron protein structures.

After several years in construction and commissioning the Macromolecular Neutron Diffractometer (MaNDi) is now operational and accepting general user proposals.

The crystallization and preliminary neutron crystallographic analysis of selectively CH₃-protonated deuterated rubredoxin from P. furiosus is presented. This work represents the first reported use of selectively labeled material for phasing applications using neutron protein crystallography.

A comparison of hydrogenous and perdeuterated haloalkane dehalogenase shows similar overall structures with only slight alterations in surface regions. However, perdeuteration causes exclusion of a critical water nucleophile from the active site leading to a structure of an inactive, low pH enzyme form.

This study reports a solution structural investigation of the Cqm1–BinB protein complex using `contrast-matched' small-angle neutron scattering (SANS). The SANS data clearly reveal that BinB binds to the receptor Cqm1 and alters its oligomeric status from a dimer to a monomer.

Perdeuteration and in vitro refolding of hen egg-white lysozyme impact protein thermal stability and activity. Deuteration appears to primarily affect enzymatic function through changes in protein dynamics, while refolding contributes to a small decrease in protein thermal stability.