The construction of a new experimental station for macromolecular crystallography at NanoTerasu under the AMED/BINDS project is presented.

This work demonstrates that multi-position data acquisition mitigates radiation damage in electron diffraction of three-dimensional protein crystals and that merging data from selected crystals in distinct orientations enhances completeness. Application of the two approaches enables high-quality structural models to be obtained from limited or sensitive samples.

YouTube video by International Union of Crystallography

Regulation of pharmaceutical lead compounds does not yet involve the need for patient-relevant macromolecular structures determined at 37°C; nevertheless, we highlight the advantages of these to ensure chemical relevance and the identification of changes which may occur under physiological conditions. The PDB and CSD entries for diffraction data measured at ≥37°C, as well as a cryoEM 37°C freeze-trapped structure, are considered and the description includes structures obtained well above 37°C that are relevant to thermophile and hyperthermophile structural biology.

In situ cryo-EM coupled with 2D template matching (2DTM) holds the potential to visualize the cellular structureome in context, but further developments are required to make this a reality. We describe Leopard-EM (Location and orientation of particles found using two-dimensional tEmplate Matching), an extensible Python package for 2DTM to accelerate in situ structural biology.

In situ cryo-EM coupled with 2D template matching (2DTM) holds the potential to visualize the cellular structureome in context, but further developments are required to make this a reality. We describ...

We present the crystal structure of a segment of human ADAMTS-5 that includes part of the cysteine-rich domain and the spacer domain.

This study presents the first crystal structure of a hydroxycinnamoyl-CoA:tartaric acid hydroxycinnamoyl transferase from E. purpurea (EpHTT), a specialized BAHD acyltransferase central to the biosynthesis of chicoric acid. We successfully expressed, purified and crystallized the full-length EpHTT protein (residues 1–424) and determined its high-resolution structure at 2.38 Å.

This article reviews the growth over the last ten years of the CCP-EM Spring Symposium. The conference is now established as a popular meeting for practitioners of life-science cryoEM and highlights new methods and exemplar applications.

Xtricorder is a tool for analysing crystallographic data, featuring a likelihood-enhanced self-rotation function and a novel `composite-section diagram' thereof, which aids interpretation and enables a machine learning-enhanced prediction of asymmetric unit content.

We present CryoLike, a user-friendly Python workflow for calculating the image-to-structure likelihood in cryo-electron microscopy.

A surface-entropy reduction approach for human Polo-like kinase 1 (PLK1) enabled a reproducible and robust crystallization system for this cancer drug target. Co-crystal structures with representatives of three different small-molecule inhibitor classes were elucidated. For two of them, co-crystal structures with PLK1 were also determined via a previously published crystallization approach using a designed ankyrin-repeat protein (DARPin), and the two approaches are compared.

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The effect of radiation damage in MicroED has been studied. By only including data collected at low accumulated electron dose during data processing, the effects of radiation damage can be reduced.

Bacteriophage ΦKZ is a massive bacterial virus with potential as a therapy for Pseudomonas aeruginosa, which forms a bacteriophage nucleus in infected cells to exclude the host immune system, and transcribes its genes with its own, non-canonical multi-subunit RNA polymerase. The structure of this polymerase in the process of binding an analogue of its cognate promoter is resolved, revealing an unanticipated method of promoter consensus recognition involving the β-like, rather than the σ-factor-like subunit.

This study presents the crystal structure of human rhinovirus (hRV)-B14 3C protease bound to AG7404, a broad-spectrum antiviral inhibitor, at a resolution of 2.11 Å. Antiviral assays and in silico studies provide structural insights into AG7404's efficacy and binding mechanism against hRV-B14, hRV-A16 and hRV-A21 3C proteases.