Model building and beyond

An introduction to the Proceedings of the 2020 CCP4 Study Weekend on model building which are available as a virtual issue at https://journals.iucr.org/special_issues/2020/CCP42020/.

Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects

Differences between the binding of RNA and DNA in S1 nuclease were analysed using X-ray crystallography. In order to properly interpret the obtained diffraction data, a correction for multiple lattice-translocation defects was applied.

Crystallographic and X-ray scattering study of RdfS, a recombination directionality factor from an integrative and conjugative element

The X-ray crystallographic structure of RdfS reveals molecular superhelical polymers in the crystal.

Dependence of crystallographic atomic displacement parameters on temperature (25–150 K) for complexes of horse liver alcohol de­hydrogenase

The crystallographic temperature factors determined for three different complexes of horse liver alcohol dehydrogenase over the range 25–150 K are relatively independent of temperature and suggest that the B factors at 100 K are relevant to catalysis at 300 K.

Substrate-induced dimerization of elaiophylin glycosyltransferase reveals a novel self-activating form of glycosyltransferase for symmetric glycosylation

The structure of the elaiophylin glycosyltransferase homodimer reveals a novel model of a self-activating form of a member of glycosyltransferase family 1 that binds the symmetric substrate.

MembraneDyn: simulating the dynamics of supported membrane stacks on the nanosecond timescale

A computational method for obtaining the time-dependent intermediate scattering function of supported membrane stacks is presented.

Structural features of chloroplast trigger factor determined at 2.6 Å resolution

This study describes the structure of the chloroplast ribosome-associated molecular chaperone trigger factor at 2.6 Å resolution. It is shown that this eukaryotic trigger factor has evolved specific structural features in plants that are distinct from those of the bacterial homolog, contributing to a better understanding of co-translational protein folding in plastids.

Structural basis for the transformation of the traditional medicine berberine by bacterial nitroreductase

The structural basis for the reduction of berberine by bacterial nitroreductases is described.