forthcoming articles

This review examines the use of ultra-small angle X-ray scattering (USAXS), a nondestructive technique for analyzing the multi-scale microstructures of hard materials such as ceramics, metals, and composites. It discusses USAXS's principles, benefits, and challenges, along with its potential to advance materials development and optimize manufacturing processes, while also considering future enhancements through multimodal characterization and machine learning.

The manuscript `Modeling a unit cell: crystallographic refinement procedure using the biomolecular MD simulation platform Amber' presents a novel protein structure refinement method claimed to offer improvements over traditional techniques like Refmac5 and Phenix. Our re-evaluation suggests that while the new method provides improvements, traditional methods achieve comparable results with less computational effort.

The determination of a challenging structure in the P1 space group, the lowest-symmetry possible, shows how our in situ serial crystallography approach expands the application of crystallization plates as a robust sample delivery method.

CrLOV1 crystalline sample was optimized for serial crystallography. Time-resolved serial synchrotron crystallography provides high-resolution insights into structural changes of CrLOV1 from Δt = 2.5 ms up to Δt = 95 ms post-photoactivation, resolving the geometry of the thio­ether adduct and alteration of the C-terminal region implicated in the signal transduction.

Time-resolved serial femtosecond crystallography experiments can be performed with samples delivered on solid supports. Sample consumption is significantly reduced when compared with the popular crystal delivery via high-viscosity extrusion.

A near-atomic resolution map was obtained for lumazine synthase while benchmarking a new microscope. At this resolution, waters, ligands and hydrogens were visible. A detailed outline of the methods used is presented that can employed for any single-particle cryo-EM experiment.

The development of CPICANN, a novel convolutional self-attention neural network, represents a groundbreaking approach in materials informatics. By leveraging the convolutional self-attention mechanism, CPICANN automates and significantly enhances the efficiency of crystal phase identification from whole X-ray powder diffraction patterns, marking a substantial advancement over traditional time-consuming methods.

In structural biology, the analogy of a key (ligand) fitting a lock (protein) is commonly used to describe the binding process. In this context, we illustrate the evolutionary development of diverse locks that exhibit specific binding to a shared key: Neu5Ac. The intricate specificity of the interaction between various locks and the common key (Neu5Ac) is explored in our review.

The 26th IUCr congress held in Melbourne brought discussions on micro-crystallization and in vivo crystallography within structural biology to the forefront, highlighting innovative approaches and collaborative efforts to advance macromolecular research.

Traditional structural models of biomolecules typically represent only a single conformational state, even though biomolecules naturally exist in multiple states crucial for their function. Here, we propose enhancements to the macromolecular crystallographic information file (mmCIF) to better capture the complex conformational and compositional heterogeneity of biomolecules that is human- and machine-interpretable.

Consensus small-angle X-ray scattering (SAXS) data from five proteins in solution generated from 171 independent measurements on 12 beamlines using a maximum likelihood method are used to benchmark computational methods for predicting SAXS profiles from atomic coordinates. The results reveal important strengths and limitations of different methods that are serving a growing community of users in applications ranging from fundamental integrative structural biology to drug discovery and development.