Nanocrystallography

Definition

Nanocrystallography (serial femtosecond crystallography) is a protein X-ray crystallography technique that uses femtosecond pulses from an X-ray free-electron laser to collect diffraction snapshots from a stream of single nano-sized crystals of a macromolecule, in order to solve a high-resolution three-dimensional macromolecular structure.

Latest Research and Reviews

  • Research |

    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
    • , Joyce Woodhouse
    • , Giorgio Schirò
    • , Virgile Adam
    • , Andrew Aquila
    • , Thomas R. M. Barends
    • , Sébastien Boutet
    • , Martin Byrdin
    • , Sergio Carbajo
    • , Eugenio De la Mora
    • , R. Bruce Doak
    • , Mikolaj Feliks
    • , Franck Fieschi
    • , Lutz Foucar
    • , Virginia Guillon
    • , Mario Hilpert
    • , Mark S. Hunter
    • , Stefan Jakobs
    • , Jason E. Koglin
    • , Gabriela Kovacsova
    • , Thomas J. Lane
    • , Bernard Lévy
    • , Mengning Liang
    • , Karol Nass
    • , Jacqueline Ridard
    • , Joseph S. Robinson
    • , Christopher M. Roome
    • , Cyril Ruckebusch
    • , Matthew Seaberg
    • , Michel Thepaut
    • , Marco Cammarata
    • , Isabelle Demachy
    • , Martin Field
    • , Robert L. Shoeman
    • , Dominique Bourgeois
    • , Jacques-Philippe Colletier
    • , Ilme Schlichting
    •  & Martin Weik
  • Research |

    A new sample-delivery method for serial X-ray crystallography exploits the full repetition rate of the X-ray free-electron laser at the LCLS facility, thus enabling efficient, high-speed data collection to solve the three-dimensional structures of viruses.

    • Philip Roedig
    • , Helen M Ginn
    • , Tim Pakendorf
    • , Geoff Sutton
    • , Karl Harlos
    • , Thomas S Walter
    • , Jan Meyer
    • , Pontus Fischer
    • , Ramona Duman
    • , Ismo Vartiainen
    • , Bernd Reime
    • , Martin Warmer
    • , Aaron S Brewster
    • , Iris D Young
    • , Tara Michels-Clark
    • , Nicholas K Sauter
    • , Abhay Kotecha
    • , James Kelly
    • , David J Rowlands
    • , Marcin Sikorsky
    • , Silke Nelson
    • , Daniel S Damiani
    • , Roberto Alonso-Mori
    • , Jingshan Ren
    • , Elizabeth E Fry
    • , Christian David
    • , David I Stuart
    • , Armin Wagner
    •  & Alke Meents
    Nature Methods 14, 805–810
  • Research |

    Crystal structures of the human GLP-1 receptor in complex with two negative allosteric modulators reveal a common binding pocket, and, together with mutagenesis and modelling studies, further our understanding of the receptor activation mechanism.Author: Please check the wording of the following statement, which will appear online only.

    • Gaojie Song
    • , Dehua Yang
    • , Yuxia Wang
    • , Chris de Graaf
    • , Qingtong Zhou
    • , Shanshan Jiang
    • , Kaiwen Liu
    • , Xiaoqing Cai
    • , Antao Dai
    • , Guangyao Lin
    • , Dongsheng Liu
    • , Fan Wu
    • , Yiran Wu
    • , Suwen Zhao
    • , Li Ye
    • , Gye Won Han
    • , Jesper Lau
    • , Beili Wu
    • , Michael A. Hanson
    • , Zhi-Jie Liu
    • , Ming-Wei Wang
    •  & Raymond C. Stevens
    Nature 546, 312–315

News and Comment