EIGER detector: application in macromolecular crystallography.

Arnau Casanas,Stefan Brandstetter,Anne Nöll,Rangana Warshamanage,Vincent Olieric,Meitian Wang,Robert Tampé,Aaron D Finke,Andreas Förster,Oliver Bunk,Clemens Schulze-Briese,Ezequiel Panepucci,Marcus Mueller

doi:10.1107/s2059798316012304

Abstract

The development of single-photon-counting detectors, such as the PILATUS, has been a major recent breakthrough in macromolecular crystallography, enabling noise-free detection and novel data-acquisition modes. The new EIGER detector features a pixel size of 75 × 75 µm, frame rates of up to 3000 Hz and a dead time as low as 3.8 µs. An EIGER 1M and EIGER 16M were tested on Swiss Light Source beamlines X10SA and X06SA for their application in macromolecular crystallography. The combination of fast frame rates and a very short dead time allows high-quality data acquisition in a shorter time. The ultrafine ϕ-slicing data-collection method is introduced and validated and its application in finding the optimal rotation angle, a suitable rotation speed and a sufficient X-ray dose are presented. An improvement of the data quality up to slicing at one tenth of the mosaicity has been observed, which is much finer than expected based on previous findings. The influence of key data-collection parameters on data quality is discussed.

Highlights

The huge improvements in the past decade in synchrotron sources, instrumentation at macromolecular crystallography (MX) beamlines, X-ray detectors, and data-processing and structure-determination software (Gruner & Lattman, 2015; Gruner et al, 2012; Smith et al, 2012; Minor et al, 2006; Kabsch, 2010a,b; Sheldrick, 2010; Adams et al, 2010) have enabled X-ray structure determination of biological macromolecules at an unprecedented pace
The new EIGER detector features a pixel size of 75 Â 75 mm, frame rates of up to 3000 Hz and a dead time as low as 3.8 ms
PILATUS detectors have been installed at many synchrotron MX beamlines worldwide

Summary

Introduction

The huge improvements in the past decade in synchrotron sources, instrumentation at macromolecular crystallography (MX) beamlines, X-ray detectors, and data-processing and structure-determination software (Gruner & Lattman, 2015; Gruner et al, 2012; Smith et al, 2012; Minor et al, 2006; Kabsch, 2010a,b; Sheldrick, 2010; Adams et al, 2010) have enabled X-ray structure determination of biological macromolecules at an unprecedented pace (http://biosync.sbkb.org). D72, 1036–1048 research papers detectors, in combination with novel diffraction goniometry and low-dose high-redundancy data-acquisition schemes, have considerably widened the range of applications for experimental phasing, native SAD, which can be considered to be a routine method (Weinert et al, 2015; Liu & Hendrickson, 2015) New experimental techniques, such as micro-crystallography (Cusack et al, 1998; Smith et al, 2012), serial crystallography (Gati et al, 2014) and room-temperature crystallography (Owen et al, 2014), continuously present new challenges that require new protocols for obtaining the most accurate and complete data while limiting the effects of radiation damage (Ravelli & Garman, 2006)

Methods

Results

Conclusion