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

Olof Svensson,Maciej Gilski,Didier Nurizzo,Matthew W Bowler

doi:10.1107/s2052252519008017

Olof Svensson, Maciej Gilski + Show 2 more

Open Access

https://doi.org/10.1107/s2052252519008017

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Abstract

The fully automatic processing of crystals of macromolecules has presented a unique opportunity to gather information on the samples that is not usually recorded. This has proved invaluable in improving sample-location, characterization and data-collection algorithms. After operating for four years, MASSIF-1 has now processed over 56 000 samples, gathering information at each stage, from the volume of the crystal to the unit-cell dimensions, the space group, the quality of the data collected and the reasoning behind the decisions made in data collection. This provides an unprecedented opportunity to analyse these data together, providing a detailed landscape of macromolecular crystals, intimate details of their contents and, importantly, how the two are related. The data show that mosaic spread is unrelated to the size or shape of crystals and demonstrate experimentally that diffraction intensities scale in proportion to crystal volume and molecular weight. It is also shown that crystal volume scales inversely with molecular weight. The results set the scene for the development of X-ray crystallography in a changing environment for structural biology.

Highlights

Macromolecular crystallography (MX) has been the primary method for the determination of biological structures over the last 70 years
The results provide the first general overview of the morphology of crystals of biological macromolecules and how these properties relate to the macromolecule itself, and this is the first study of its kind in the history of macromolecular crystallography
The data collected for all samples processed on MASSIF-1 provide an opportunity, for the first time, to define the broad distribution of protein crystal dimensions

Summary

Introduction

Macromolecular crystallography (MX) has been the primary method for the determination of biological structures over the last 70 years. The deposited data represent probably the best data that were obtained for a sample and were, as such, the result of extensive screening, thereby hiding the potentially thousands of crystals that stand behind the final structure. Experimental details, such as the size, shape and quality variation of the crystals, the data-collection strategy etc., are often lost, even if recorded in the primary citation.

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