20 years of crystal hits: progress and promise in ultrahigh-throughput crystallization screening

The crystallization facility at Hauptman–Woodward Medical Research Institute, now the National High-Throughput Crystallization Center, has served the structural biology community for over two decades. The lessons learned from our high-throughput crystallization services, current operations and capabilities are described, together with a vision for the future of crystallization.

Errors in structural biology are not the exception

Errors from measurement, data processing and modelling are present throughout structures deposited in the Protein Data Bank. Identifying them is only the first step. What needs to change in order to minimize their impact?

Obtaining anomalous and ensemble information from protein crystals from 220 K up to physiological temperatures

Anomalous information was obtained from model lysozyme, thaumatin and proteinase K crystals from 220 K up to physiological temperatures.

Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect

Correction of serial crystallography diffraction intensities for lattice-translocation defects enabled the interpretation of time-resolved serial femtosecond crystallography data probing the first molecular motions in vertebrate vision.

Accelerating crystal structure determination with iterative AlphaFold prediction

AlphaFold predictions can be used both as a starting point for structure determination and as a method of model optimization. The Phenix PredictAndBuild tool automates iterative prediction and model building, yielding a density map and model starting with sequence information and crystallographic data.

Structural basis of DNA binding by YdaT, a functional equivalent of the CII repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7

YdaT, a functional equivalent of the bacteriophage λ CII repressor in certain lambdoid phages, is a member of the POU-domain family and recognizes a 5′-TTGATTN₆AATCAA-3′ inverted repeat.

A tetramerization domain in prokaryotic and eukaryotic transcription regulators homologous to p53

The tetramerization domain of the bacterial gene repressor Rco from Bacillus subtilis plasmid pLS20 was identified. The structure shows high similarity to the tetramerization domain of the p53 family of human tumor suppressors, despite having low sequence homology.