Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–11 of 11 results
Advanced filters: Author: Nicolas Coquelle Clear advanced filters

  • rsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolution light microscopy. Here the authors present the structure of an rsEGFP2 ground-state intermediate after excited state-decay that was obtained by nanosecond time-resolved serial femtosecond crystallography at an X-ray free electron laser, and time-resolved absorption spectroscopy measurements complement their structural analysis.

    • Joyce Woodhouse
    • Gabriela Nass Kovacs
    • Martin Weik
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Providing detailed structural descriptions of the ultrafast photochemical events that occur in light-sensitive proteins is key to their understanding. Now, excited-state structures in the reversibly switchable fluorescent protein rsEGFP2 have been solved by time-resolved crystallography using an X-ray laser. These structures enabled the design of a mutant with improved photoswitching quantum yields.

    • Nicolas Coquelle
    • Michel Sliwa
    • Martin Weik
    Research
    Nature Chemistry
    Volume: 10, P: 31-37

  • New structural analyses suggest two different models for poly(ADP-ribose) polymerase 1 (PARP1) activation by single- and double-strand DNA breaks, providing evidence for PARP1 activation in cis and in trans.

    • Nicolas Coquelle
    • J N Mark Glover
    News & Views
    Nature Structural & Molecular Biology
    Volume: 19, P: 660-661

  • An environmentally safe means of mosquito control is the application of Bacillus thuringiensis israelensis, which produces a cocktail of four naturally crystalline proteins exclusively toxic to mosquito. Here the authors report the atomic-resolution structures of Bti Cry11Aa and related Btj Cry11Ba solved de novo through Serial Femtosecond Crystallography on naturally-occurring nanocrystals.

    • Guillaume Tetreau
    • Michael R. Sawaya
    • Jacques-Philippe Colletier
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • Bacillus thuringiensis israelensis (Bti) produces the naturally-crystalline proteinaceous toxin Cyt1Aa that is toxic to mosquito larvae. Here the authors grow recombinant nanocrystals of the Cyt1Aa protoxin in vivo and use serial femtosecond crystallography to determine its structure at different redox and pH conditions and by combining their structural data with further biochemical, toxicological and biophysical analyses provide mechanistic insights into the Cyt1Aa bioactivation cascade.

    • Guillaume Tetreau
    • Anne-Sophie Banneville
    • Jacques-Philippe Colletier
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16

  • The structure of the bacterial toxin BinAB, which is used to combat mosquito-borne diseases, reveals pH-sensitive switches and carbohydrate-binding modules that may contribute to the larvicidal function of the toxin.

    • Jacques-Philippe Colletier
    • Michael R. Sawaya
    • David S. Eisenberg
    Research
    Nature
    Volume: 539, P: 43-47

  • Small-amplitude overall motion of molecules in crystals limits the achievable resolution in X-ray diffraction, yet little is known about its exact nature. Here, the authors obtain NMR, XRD and MD data from three different crystal forms of a protein (ubiquitin) to gain insight into amplitude and timescale of such motions.

    • Peixiang Ma
    • Yi Xue
    • Paul Schanda
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-10

  • X-ray crystallography is the main method for protein structure determination. Here the authors combine solid-state NMR measurements and molecular dynamics simulations and show that crystal packing alters the thermodynamics and kinetics of local conformational exchange as well as overall rocking motion of protein molecules in the crystal lattice.

    • Vilius Kurauskas
    • Sergei A. Izmailov
    • Paul Schanda
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-12

  • Serial macromolecular crystallography has become a powerful method to reveal room-temperature structures of biological macromolecules and perform time-resolved studies, however, the experiments remain complex and challenging for broader applications. Here, the authors develop serial microsecond crystallography using high-brilliance, high-repetition-rate X-ray pulses at the newly constructed ID29 beamline of the ESRF-EBS 4th generation synchrotron, featuring microsecond exposure times, innovative beam characteristics, adaptable sample environment, and high-quality complete data.

    • Julien Orlans
    • Samuel L. Rose
    • Daniele de Sanctis
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-12