New Section Editor of Acta Cryst. D

Introducing the new Section Editor of Acta Cryst. D.

Fragment-based determination of a proteinase K structure from MicroED data using ARCIMBOLDO_SHREDDER

A 1.6 Å resolution MicroED data set of proteinase K is phased using fragments derived from distantly related sequence homologues. ARCIMBOLDO_SHREDDER expands the phasing options for MicroED applications, overcoming the need for complete and highly accurate search models.

Predicting protein model correctness in Coot using machine learning

Two neural networks were trained to predict the correctness of protein residues by combining multiple validation metrics in Coot. Using the predicted correctness to automatically prune models led to significant improvements in the Buccaneer pipeline.

Combining high throughput and high quality for cryo-electron microscopy data collection

Methods for obtaining the maximum out of a cryo-EM data-collection session are described.

Structure of the HLTF HIRAN domain and its functional implications in regression of a stalled replication fork

Based on crystal structures of HIRAN in complex with duplex DNA, the mechanism of replication-fork regression underlying the sequence-independent recognition of nucleobases by HIRAN is discussed.

Evaluating crystallographic likelihood functions using numerical quadratures

A quadrature is developed that allows the efficient evaluation of an intensity-based likelihood target function that includes experimental errors.

Attaining atomic resolution from in situ data collection at room temperature using counter-diffusion-based low-cost microchips

The benefits are shown of combining a high-density protein-crystallization technique (counter-diffusion) with in situ room-temperature data collection at synchrotron sources as an approximation to serial crystallography, without compromising data quality.

Novel structure of the N-terminal helical domain of BibA, a group B streptococcus immunogenic bacterial adhesin

The X-ray crystallographic structure of an N-terminal fragment of group B streptococcus BibA (BibA_126–398) and a low-resolution structure of the full-length N-terminal domain (BibA_34–400) determined using small-angle X-ray scattering are described. The association of the N-terminal domain of BibA was localized to the C4BP α-chain.

FragMAX: the fragment-screening platform at the MAX IV Laboratory

FragMAX is the fragment-screening platform of BioMAX, the macromolecular crystallography beamline of the MAX IV Laboratory. It provides support for users during sample preparation, data collection and data analysis through its in-house-developed software, FragMAXapp.

Structural and biochemical characterization of a gluta­thione transferase from the citrus canker pathogen Xanthomonas

Crystal structures of XacGST, a glutathione S-transferase from the citrus canker pathogen Xanthomonas citri subsp. citri, with and without glutathione are reported.

High-throughput in situ experimental phasing

A new procedure for experimental phasing at room temperature using diffraction data collected directly from the crystallization plates is described, demonstrated and tested.