Crystal structure of a covalently linked Aurora-A–MYCN complex

The crystal structure of a covalently linked Aurora-A–MYCN complex is reported, enabling drug design and screening studies.

Protein model refinement for cryo-EM maps using AlphaFold2 and the DAQ score

A new protocol, DAQ-refine, for evaluating a protein model built from a cryo-EM map and applying local structure refinement is described.

Drosophila melanogaster frataxin: protein crystal and predicted solution structure with identification of the iron-binding regions

The structure of Drosophila melanogaster frataxin (Dfh) was derived by X-ray crystallography and studied by NMR spectroscopy. The crystal and solution structures are extremely similar. NMR spectroscopy was also used to identify the iron-binding location on helix 1 and strand 1 of Dfh.

A scoring function for the prediction of protein complex interfaces based on the neighborhood preferences of amino acids

A scoring function has been developed for the prediction of protein complex interfaces based on neighboring amino acids.

Structures of permuted halves of a modern ribose-binding protein

The crystal structures of two permuted halves of a ribose-binding protein from Thermotoga maritima provide insights into the evolution of the periplasmic binding protein fold from a flavodoxin-like precursor by duplication and domain swapping.

Molecular-dynamics simulation methods for macromolecular crystallography

Atomistic simulations enhance protein crystallography, yielding mechanistic insights into a protein kinase involved in the regulation of fundamental biological processes that include metabolism, development, memory and immune response.

Structural insights into the effects of glycerol on ligand binding to cytochrome P450

This work shows that glycerol may compromise functional assays and crystallographic studies of pharmacological protein targets, consequently lowering the success rate of drug-discovery campaigns.

Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization

Key physical principles and methods for collecting crystallographic data from biomolecular systems at room temperature and, more generally, at temperatures between ∼200 and ∼350 K are reviewed and discussed.