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 1–17 of 17 results
Advanced filters: Author: Raimund Fromme Clear advanced filters

  • Due to the pulsed nature of X-ray free electron laser (XFEL) instruments the majority of protein crystals, which are injected using continuous jet injection techniques are wasted. Here, the authors present a microfluidic device to deliver aqueous protein crystal laden droplets segmented with an immiscible oil and demonstrate that with this device an approx. 60% reduction in sample waste was achieved for data collection of 3-deoxy-D-manno-octulosonate 8-phosphate synthase crystals at the EuXFEL.

    • Austin Echelmeier
    • Jorvani Cruz Villarreal
    • Alexandra Ros
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • The European X-ray free-electron laser (EuXFEL) in Hamburg is the first XFEL with a megahertz repetition rate. Here the authors present the 2.9 Å structure of the large membrane protein complex Photosystem I from T. elongatus that was determined at the EuXFEL.

    • Chris Gisriel
    • Jesse Coe
    • Nadia A. Zatsepin
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • Serial femtosecond X-ray crystallography permits the use of very small protein crystals; however, a continuous flow of sample is required. Weierstall et al. design and demonstrate an injector system that can supply microcrystals in the lipidic cubic phase, dramatically reducing the quantities of protein required.

    • Uwe Weierstall
    • Daniel James
    • Vadim Cherezov
    Research
    Nature Communications
    Volume: 5, P: 1-6

  • Serial femtosecond crystallography is an X-ray free-electron-laser-based method that uses X-ray bursts to determine protein structures. Here the authors present the structure of a photosynthetic reaction centre, an integral membrane protein, achieved with no sign of X-ray-induced radiation damage.

    • Linda C. Johansson
    • David Arnlund
    • Richard Neutze
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-7

  • Diacylglycerol kinase is a small bacterial membrane-bound trimer that catalyses diacylglycerol conversion to phosphatidic acid. Here, the authors solve the crystal structure of the kinase bound to a lipid substrate and an ATP analogue, and show that the active site arose through convergent evolution.

    • Dianfan Li
    • Phillip J. Stansfeld
    • Martin Caffrey
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-12

  • G protein-coupled receptors are a large family of signalling proteins that mediate cellular responses primarily via G proteins or arrestins, and they are targets of one-third of the current clinically used drugs; here, an active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin-1 is determined, revealing unique structural features that may constitute essential elements for arrestin-biased signalling.

    • Yanyong Kang
    • X. Edward Zhou
    • H. Eric Xu
    Research
    Nature
    Volume: 523, P: 561-567

  • The start-up of the new femtosecond hard X-ray laser facility in Stanford, the Linac Coherent Light Source, has brought high expectations for a new era for biological imaging. The intense, ultrashort X-ray pulses allow diffraction imaging of small structures before radiation damage occurs. This new capability is tested for the problem of structure determination from nanocrystals of macromolecules that cannot be grown in large crystals. Over three million diffraction patterns were collected from a stream of nanocrystals of the membrane protein complex photosystem I, which allowed the assembly of a three-dimensional data set for this protein, and proves the concept of this imaging technique.

    • Henry N. Chapman
    • Petra Fromme
    • John C. H. Spence
    Research
    Nature
    Volume: 470, P: 73-77

  • Serial femtosecond crystallography of the human δ-opioid receptor in complex with an endomorphin-derived peptide reveals interactions that are important for understanding the pharmacology of opioid peptides and developing analgesics with reduced side effects.

    • Gustavo Fenalti
    • Nadia A Zatsepin
    • Vadim Cherezov
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 265-268

  • Crystal lattice disorder, which gives rise to a continuous diffraction pattern, is exploited to determine the structure of the integral membrane protein complex photosystem II to a higher resolution than could be achieved using Bragg diffraction alone.

    • Kartik Ayyer
    • Oleksandr M. Yefanov
    • Henry N. Chapman
    Research
    Nature
    Volume: 530, P: 202-206

  • Femtosecond X-ray pulses were used to obtain diffraction data on photosystem II, revealing conformational changes as the complex transitions from the dark S1 state to the double-pumped S3 state; the time-resolved serial femtosecond crystallography technique enables structural determination of protein conformations that are highly prone to traditional radiation damage.

    • Christopher Kupitz
    • Shibom Basu
    • Petra Fromme
    Research
    Nature
    Volume: 513, P: 261-265