Diverse application platform for hard X-ray diffraction in SACLA (DAPHNIS): application to serial protein crystallography using an X-ray free-electron laser.

Kensuke Tono,Tomoyuki Tanaka,Mamoru Suzuki,Eriko Nango,Takashi Kameshima,Rie Tanaka,Jaehyun Park,Michihiro Sugahara,Takaki Hatsui,So Iwata,Tatsuro Shimamura,Changyong Song,Yasumasa Joti,Yoshiki Tanaka,Eiichi Mizohata,Makina Yabashi,Shun Ono

doi:10.1107/s1600577515004464

Abstract

An experimental system for serial femtosecond crystallography using an X-ray free-electron laser (XFEL) has been developed. It basically consists of a sample chamber, fluid injectors and a two-dimensional detector. The chamber and the injectors are operated under helium atmosphere at 1 atm. The ambient pressure operation facilitates applications to fluid samples. Three kinds of injectors are employed to feed randomly oriented crystals in aqueous solution or highly viscous fluid. Experiments on lysozyme crystals were performed by using the 10 keV XFEL of the SPring-8 Angstrom Compact free-electron LAser (SACLA). The structure of model protein lysozyme from 1 µm crystals at a resolution of 2.4 Å was obtained.

Highlights

An X-ray free-electron laser (XFEL) offers opportunities for high-resolution structure analysis using X-ray pulses with a large number of photons and a short duration (Emma et al, 2010; Ishikawa et al, 2012)
In this paper we describe the design and performance of the experimental platform DAPHNIS (Diverse Application Platform for Hard X-ray diffractioN In SPring-8 Angstrom Compact free-electron LAser (SACLA)), which is dedicated for SFX at SACLA in order to facilitate the measurement of a wide variety of samples
The experimental system DAPHNIS has been successfully applied to SFX of proteins

Summary

Introduction

An X-ray free-electron laser (XFEL) offers opportunities for high-resolution structure analysis using X-ray pulses with a large number of photons and a short duration (Emma et al, 2010; Ishikawa et al, 2012). The SPring-8 Angstrom Compact free-electron LAser (SACLA) provides $1011 photons in a pulse with a duration shorter than 10 fs These characteristics are advantageous in application for protein crystallography, as even a single XFEL pulse can provide enough photons for recording a diffraction pattern from a protein crystal. Serial femtosecond crystallography (SFX) has been developed at the Linac Coherent Light Source (LCLS) for recording a considerable number of damage-free diffraction patterns from tiny crystals (Chapman et al, 2011; Boutet et al, 2012). This method often adopts a fluid carrier to continuously feed crystals of micrometer sizes and with random orientations.

Methods

Results

Conclusion