학술논문

Membrane protein megahertz crystallography at the European XFEL
Document Type
article
Source
Nature Communications. 10(1)
Subject
Biochemistry and Cell Biology
Biological Sciences
1.1 Normal biological development and functioning
Underpinning research
Generic health relevance
Crystallography
Cyanobacteria
Electrons
Lasers
Membrane Proteins
Models
Molecular
Photosystem I Protein Complex
Static Electricity
Synchrotrons
Thermosynechococcus
X-Rays
Language
Abstract
The world's first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.