January 2023 issue
The crystal structure of a covalently linked Aurora-A–MYCN complex is reported, enabling drug design and screening studies.
A new protocol, DAQ-refine, for evaluating a protein model built from a cryo-EM map and applying local structure refinement is described.
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 has been developed for the prediction of protein complex interfaces based on neighboring amino acids.
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.
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.
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.
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.