Serial femtosecond crystallography: the first five years

I Schlichting - IUCrJ, 2015 - journals.iucr.org
Protein crystallography using synchrotron radiation sources has had a tremendous impact
on biology, having yielded the structures of thousands of proteins and given detailed insight …

MOFs in the time domain

DJ Cerasale, DC Ward, TL Easun - Nature Reviews Chemistry, 2022 - nature.com
Many of the proposed applications of metal–organic framework (MOF) materials may fail to
materialize if the community does not fully address the difficult fundamental work needed to …

Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses

M Suga, F Akita, K Hirata, G Ueno, H Murakami… - Nature, 2015 - nature.com
Photosynthesis converts light energy into biologically useful chemical energy vital to life on
Earth. The initial reaction of photosynthesis takes place in photosystem II (PSII), a 700 …

High-resolution protein structure determination by serial femtosecond crystallography

S Boutet, L Lomb, GJ Williams, TRM Barends, A Aquila… - Science, 2012 - science.org
Structure determination of proteins and other macromolecules has historically required the
growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding …

Megahertz serial crystallography

MO Wiedorn, D Oberthür, R Bean, R Schubert… - Nature …, 2018 - nature.com
The new European X-ray Free-Electron Laser is the first X-ray free-electron laser capable of
delivering X-ray pulses with a megahertz inter-pulse spacing, more than four orders of …

MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography

MTB Clabbers, S Holmes, TW Muusse… - Nature …, 2021 - nature.com
MyD88 and MAL are Toll-like receptor (TLR) adaptors that signal to induce pro-inflammatory
cytokine production. We previously observed that the TIR domain of MAL (MALTIR) forms …

Diffraction before destruction

HN Chapman, C Caleman… - … Transactions of the …, 2014 - royalsocietypublishing.org
X-ray free-electron lasers have opened up the possibility of structure determination of
protein crystals at room temperature, free of radiation damage. The femtosecond-duration …

[PDF][PDF] Radiation damage in macromolecular crystallography: what is it and why should we care?

EF Garman - Acta Crystallographica Section D: Biological …, 2010 - journals.iucr.org
Radiation damage inflicted during diffraction data collection in macromolecular
crystallography has re-emerged in the last decade as a major experimental and …

Determination of damage-free crystal structure of an X-ray–sensitive protein using an XFEL

K Hirata, K Shinzawa-Itoh, N Yano, S Takemura… - Nature …, 2014 - nature.com
We report a method of femtosecond crystallography for solving radiation damage–free
crystal structures of large proteins at sub-angstrom spatial resolution, using a large single …

[PDF][PDF] Room-temperature macromolecular serial crystallography using synchrotron radiation

F Stellato, D Oberthür, M Liang, R Bean, C Gati… - IUCrJ, 2014 - journals.iucr.org
A new approach for collecting data from many hundreds of thousands of microcrystals using
X-ray pulses from a free-electron laser has recently been developed. Referred to as serial …