Fully automatic macromolecular crystallography: the impact of MASSIF-1 on the optimum acquisition and quality of data

Abstract

Automation is beginning to transform the way data are collected in almost all scientific disciplines. The combination of robotics and software now allows data to be collected consistently and reproducibly, eliminating human error and boredom. This approach has been applied to macromolecular crystallography at MASSIF-1, a fully automated beamline at the European Synchrotron Radiation Facility (ESRF). Considerable human effort is still dedicated to evaluating protein crystals in order to find the few crystals that diffract well or collecting hundreds of data sets to screen potential new drug candidates. The combination of ESRF-developed robotic sample handling and advanced software protocols now provides a new tool to structural biologists. Not only is the beamline used efficiently, running 24 h a day without getting tired, data collection is also performed consistently by an expert system, often better than with a human operator. In this review, we will focus on the impact this level of automation has had on the optimum acquisition of data from crystals of biological macromolecules.

A comparative anatomy of protein crystals: lessons from the automatic processing of 56,000 samples

“…Accurately determining the dimensions, and therefore volumes, of a protein crystal is primarily important in determining the dose that the crystal can absorb before significant radiation damage (Bourenkov & Popov, 2010;Bowler et al, 2016;Svensson et al, 2015;Zeldin et al, 2013) and…”

A Research on Use of Robotics In High Rise Buildings

“…Nevertheless, this SCF's apparatus arrangement restricts the versatility of construction methods that are automated. Furthermore, weights and the costs are high on account of these robots' mixture cranes and lifting processes [12,13]. Hence, Kang et al [1][2] established a robotic-crane established automatic structure technique (r-a platform) for metal constructions of high tech structures, that contains a structure mill (CF), also a steel gathering platform and also a tracking and management platform.…”

RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments

“…of crystals from users, including one with dimensions of 28 Â 57 Â 13 mm, which is indicative of the accuracy of the device (Bowler et al, 2016).…”

“…Since receiving user samples, data collections have been performed on many types of crystal, from well characterized systems all the way to weakly diffracting crystals (Koromyslova et al, 2015;Neudegger et al, 2016;Papageorgiou et al, 2016;Thierry et al, 2016), with the smallest crystal having a volume of only 20 748 mm 3 (28 Â 57 Â 13 mm; Bowler et al, 2016), and 20 structures have been solved de novo to date (see, for example, Kharde et al, 2015;Muir et al, 2016). In combination with software routines that locate, centre and collect data (Svensson et al, 2015), the RoboDiff has proved to not only be the cornerstone of complete automation but is also an instrument that can collect high-quality data from samples.…”

“…Careful attention has also been paid to sample identification, which is essential for automated user-free data collection. The Robo-Diff forms the core of the services offered on the ESRF beamline MASSIF-1 (Bowler et al, 2015(Bowler et al, , 2016Svensson et al, 2015) and, thus far, has been used to mount, characterize and collect diffraction data from over 20 000 samples since September 2014. Schematic of the RoboDiff, HCD and experiment environment on MASSIF-1.…”