5FXN
Structure of thermolysin solved by SAD from data collected by Direct Data Collection (DDC) using the ESRF RoboDiff goniometer
Summary for 5FXN
Entry DOI | 10.2210/pdb5fxn/pdb |
Related | 5FXL 5FXM |
Descriptor | THERMOLYSIN, VALINE, LYSINE, ... (6 entities in total) |
Functional Keywords | hydrolase |
Biological source | BACILLUS THERMOPROTEOLYTICUS |
Total number of polymer chains | 1 |
Total formula weight | 34739.21 |
Authors | Bowler, M.W.,Nurizzo, D. (deposition date: 2016-03-02, release date: 2016-03-16, Last modification date: 2024-05-08) |
Primary citation | Nurizzo, D.,Bowler, M.W.,Caserotto, H.,Dobias, F.,Giraud, T.,Surr, J.,Guichard, N.,Papp, G.,Guijarro, M.,Mueller-Dieckmann, C.,Flot, D.,Mcsweeney, S.,Cipriani, F.,Theveneau, P.,Leonard, G.A. Robodiff: Combining a Sample Changer and Goniometer for Highly Automated Macromolecular Crystallography Experiments. Acta Crystallogr.,Sect.D, 72:966-, 2016 Cited by PubMed Abstract: Automation of the mounting of cryocooled samples is now a feature of the majority of beamlines dedicated to macromolecular crystallography (MX). Robotic sample changers have been developed over many years, with the latest designs increasing capacity, reliability and speed. Here, the development of a new sample changer deployed at the ESRF beamline MASSIF-1 (ID30A-1), based on an industrial six-axis robot, is described. The device, named RoboDiff, includes a high-capacity dewar, acts as both a sample changer and a high-accuracy goniometer, and has been designed for completely unattended sample mounting and diffraction data collection. This aim has been achieved using a high level of diagnostics at all steps of the process from mounting and characterization to data collection. The RoboDiff has been in service on the fully automated endstation MASSIF-1 at the ESRF since September 2014 and, at the time of writing, has processed more than 20 000 samples completely automatically. PubMed: 27487827DOI: 10.1107/S205979831601158X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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