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 | | open

    X-ray free-electron lasers produce bright femtosecond X-ray pulses. Here, the authors use a two-colour X-ray free-electron laser beam for simultaneous two-wavelength data collection and show that protein structures can be determined with multiple wavelength anomalous dispersion phasing, which is important for difficult-to-phase projects.

    • Alexander Gorel
    • , Koji Motomura
    • , Hironobu Fukuzawa
    • , R. Bruce Doak
    • , Marie Luise Grünbein
    • , Mario Hilpert
    • , Ichiro Inoue
    • , Marco Kloos
    • , Gabriela Kovácsová
    • , Eriko Nango
    • , Karol Nass
    • , Christopher M. Roome
    • , Robert L. Shoeman
    • , Rie Tanaka
    • , Kensuke Tono
    • , Yasumasa Joti
    • , Makina Yabashi
    • , So Iwata
    • , Lutz Foucar
    • , Kiyoshi Ueda
    • , Thomas R. M. Barends
    •  & Ilme Schlichting
  • Research | | open

    Chaperonins (CPNs) are ATP-dependent protein-folding machines. Here the authors present the open and closed crystal structures of a Group III CPN from the thermophilic bacterium Carboxydothermus hydrogenoformans, discuss its mechanism and structurally compare it with Group I and II CPNs.

    • Young Jun An
    • , Sara E. Rowland
    • , Jung-Hyun Na
    • , Dario Spigolon
    • , Seung Kon Hong
    • , Yeo Joon Yoon
    • , Jung-Hyun Lee
    • , Frank T. Robb
    •  & Sun-Shin Cha
  • 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

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