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Search query: blue-light photoreceptors
17 articles match your search "blue-light photoreceptors"Results 1 to 10, sorted by relevance:
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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This article gives an overview of current trends and challenges in serial crystallography, with a focus on results from time-resolved experiments.
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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.