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. 2015 Dec;11(12):895-9.
doi: 10.1038/nchembio.1968.

XFELs open a new era in structural chemical biology

Petra Fromme  1
Affiliations

XFELs open a new era in structural chemical biology

Petra Fromme. Nat Chem Biol. 2015 Dec.

Abstract

X-ray crystallography, the workhorse of structural biology, has been revolutionized by the advent of serial femtosecond crystallography using X-ray free electron lasers. Here, the fast pace and history of discoveries are discussed together with current challenges and the method’s great potential to make new structural discoveries, such as the ability to generate molecular movies of biomolecules at work.

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Conflict of interest statement

Competing financial interests

The author declares no competing financial interests.

Figures

Figure 1
Figure 1
Schematic picture of collection of time-resolved data with SFX crystallography. Crystals are delivered to the X-ray beam in a liquid jet. The structure is probed by femtosecond X-ray pulses from a free electron laser. The time domain is added to the X-ray diffraction experiment by triggering of a reaction by light, where the reaction progression is monitored by variation of the time delay between optical ‘pump’ pulse and the X-ray pulse. Figure modified from ref. .
Figure 2
Figure 2
Highlights of structures of membrane proteins solved by SFX. (a) Photosystem I. (b) Photosystem II. (c) β-adrenergic receptor. (d) Smoothened receptor. (e) Opinoid receptor. (f) Angiotensin receptor. (g) Rhodopsin–arrestin complex. Images reproduced from refs. (a), (b), (d) (e) and (g) and, with permission, from ref. (c) and ref. (f).
Figure 3
Figure 3
Comparison of time-resolved Laue crystallography and time-resolved SFX crystallography. Left, Laue crystallography; right, time-resolved SFX. Examples are shown here for PYP. The diffraction patterns and the crystal photo were kindly provided by M. Schmidt. Electron density data are reproduced with permission from ref. .
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