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Nurizzo, D.

Publications and source records attributed to Nurizzo, D..

3 recordsLinked to original sources

In-situ serial crystallography facilitates 96-well plate structuralanalysis at low symmetry

The advent of serial crystallography has rejuvenated and popularised room temperature X-ray crystal structure determination. Structures determined at physiological temperature reveal protein flexibility and dynamics. In addition, challenging samples (e.g., large complexes, membrane proteins, and viruses) forming fragile crystals, are often difficult to harvest for cryo-crystallography. Moreover, a typical serial crystallography experiment requires a large number of microcrystals, mainly achievable through batch crystallisation. Many medically relevant samples are expressed in mammalian cell-lines, producing a meagre quantity of protein that is incompatible for batch crystallisation. This can limit the scope of serial crystallography approaches. Direct in-situ data collection from a 96-well crystallisation plate enables not only the identification of the best diffracting crystallisation condition, but also the possibility for structure determination at ambient conditions. Here, we describe an in situ serial crystallography (iSX) approach, facilitating direct measurement from crystallisation plates, mounted on a rapidly exchangeable universal plate holder deployed at a microfocus beamline, ID23-2, at the European Synchrotron Radiation Facility (ESRF). We applied our iSX approach on a challenging project, Autotaxin, a therapeutic target expressed in a stable human cell-line, to determine a structure in the lowest symmetry P1 space group at 3.0 [A] resolution. Our in situ data collection strategy provided a complete dataset for structure determination, while screening various crystallisation conditions. Our data analysis reveals that the iSX approach is highly efficient at a microfocus beamline, improving throughput and demonstrating how crystallisation plates can be routinely used as an alternative method of presenting samples for serial crystallography experiments at synchrotrons. SynopsisThe determination of a challenging structure in the P1 space group, the lowest symmetry possible, shows how our in-situ serial crystallography approach expands the application of crystallisation plates as a robust sample delivery method.

biophysics↗

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

SynopsisThe automatic processing of over 56,000 crystals by the autonomous ESRF beamline MASSIF-1 has provided a data set of crystal characteristics and properties that allows many theoretical proposals and assumptions to be evaluated experimentally. AbstractThe 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 the sample location, characterisation 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, space group, 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 and 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.

biophysics↗

Recent improvements to the automatic characterization and data collection algorithms on MASSIF-1

Macromolecular crystallography (MX) is now a mature and widely used technique essential in the understanding of biology and medicine. Increases in computing power combined with robotics have enabled not only large numbers of samples to be screened and characterised but also for better decisions to be taken on data collection itself. This led to the development of MASSIF-1 at the ESRF, the worlds first beamline to run fully automatically while making intelligent decisions taking user requirements into account. Since opening in late 2014 the beamline has now processed over 39,000 samples. Improvements have been made to the speed of the sample handling robotics and error management within the software routines. The workflows initially put in place, while highly innovative at the time, have been expanded to include increased complexity and additional intelligence using the information gathered during characterisation, this includes adapting the beam diameter dynamically to match the diffraction volume within the crystal. Complex multi-position and multi-crystal data collections are now also integrated into the selection of experiments available. This has led to increased data quality and throughput allowing even the most challenging samples to be treated automatically.\n\nSynopsis\n\nSignificant improvements in the sample location, characterisation and data collection algorithms on the autonomous ESRF beamline MASSIF-1 are described. The workflows now include dynamic beam diameter adjustment and multi-position and multi-crystal data collections.

molecular biology↗