A method is presented to perform time-resolved X-ray crystallography with a 63 ms time resolution using a fast pixel detector and partial oscillation data sets. This minimizes the number of crystals (<100) required for a complete experiment.

The crystallization of the LOV domain of the blue-light receptor YtvA from B. amyloliquefaciens FZB42 is described. The crystals diffracted to 1.60 Å resolution.

A crystalline sample of CrLOV1 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.

The X-ray structure of the light, oxygen or voltage domain 2 of phototropin 1 from A. thaliana (AtLOV2) in its dark-adapted state has been determined. The N-terminal flanking A′α helix of AtLOV2 plays a role in its dimerization.

The photo-reaction of the LOV1 domain of the Chlamydomonas reinhardtii phototropin is investigated by room-temperature time-resolved serial crystallography. A covalent adduct forms between the C4a atom of the central flavin-mononucleotide chromophore and a protein cysteine. The structure of the adduct is very similar to that of LOV2 determined 23 years ago from the maidenhair fern Phy3.

The crystal structure of the response regulator RPA3017 from the photosynthetic bacterium R. palustris has been determined at 1.9 Å resolution. RPA3017 is part of a two-component system that involves two tandem bacteriophytochromes involved in red-light signaling.

High-resolution X-ray diffraction data were collected at room temperature for light- and dark-adapted states of the archaerhodopsin-3 photoreceptor using transparent and opaque polymer-film sample mounts.

The chromophore-binding domain of cyanobacteriochrome AnPixJ was overproduced in E. coli, purified and crystallized in its red-absorbing form. Diffraction data were then collected to a resolution of 1.8 Å.

This article gives an overview of current trends and challenges in serial crystallography, with a focus on results from time-resolved experiments.

Ambiguities in and the completeness of SAS data analysis of membrane proteins (MPs) are considered here in the case of the sensory rhodopsin II–transducer complex solubilized in a detergent. The contribution of the detergent belt surrounding MPs is one of the main problems in SAS data analysis of MPs; the second problem addressed here is the influence of oligomerization polydispersity (which is a sufficiently common phenomenon for MPs) on the quality of SAS structural analysis.