Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser

• DOI: 10.1073/pnas.1609243114
• Publication Date: 2017-02-16T02:10:46Z
• Authors: Cornelius Gati; Dominik Oberthuer; Oleksandr Yefanov; Richard D. Bunker; Francesco Stellato; Elaine Chiu; Shin-Mei Yeh; Andrew Aquila; Shibom Basu; Richard Bean; Kenneth R. Beyerlein; Sabine Botha; Sébastien Boutet; Daniel P. DePonte; R. Bruce Doak; Raimund Fromme; Lorenzo Galli; Ingo Grotjohann; Daniel R. James; Christopher Kupitz; Lukas Lomb; Marc Messerschmidt; Karol Nass; Kimberly Rendek; Robert L. Shoeman; Dingjie Wang; Uwe Weierstall; Thomas A. White; Garth J. Williams; Nadia A. Zatsepin; Petra Fromme; John C. H. Spence; Kenneth N. Goldie; Johannes A. Jehle; Peter Metcalf; Anton Barty; Henry N. Chapman
• Keywords: Nanocrystalline material

Significance The room temperature structure of natively formed protein nanocrystals consisting 9,000 unit cells has been solved to 2 Å resolution using an unattenuated X-ray free-electron laser (XFEL) beam, representing, by far, the smallest crystals used for determination crystallography date. Radiation damage limits from synchrotron techniques, whereas femtosecond pulses lasers enable much higher tolerable doses, extracting more signal per molecule, allowing study submicrometer crystals. Radiation-sensitive features, such as disulfide bonds, are well resolved in XFEL despite extremely high dose (1.3 GGy) used. Analysis levels obtained this experiment indicates that even smaller could be possible.