Raw diffraction data (CBF) for a structure of SARS-CoV-2 Main Protease bound to 2-Methyl-1-tetralone

Data collected at beamline P11/PETRAIII Deutsches Elektronen Synchrotron DESY Info: run type: regular<br> run name: l6p17_09_001<br> start angle: 0.000000deg<br> frames: 1000<br> degrees/frame: 0.200000deg<br> exposure time: 40.000000ms<br> energy: 11.999832keV<br> wavelength: 1.033214A<br> detector distance: 200.000000mm<br> resolution: 1.304257A<br> aperture: 100um<br> filter transmission: 71.798748%<br> filter thickness: 75um<br> ring current: 119.222664mA Crystal-info: Co-crystallization of Sars-CoV-2 MPro with the compound was achieved by equlibrating a 6.25 mg/ml protein solution in 20 mM HEPES buffer (pH 7.8) containing 1 mM DTT, 1mM EDTA, and 150 mM NaCl against a reservoir solution of 100 mM MIB buffer (2:3:3 molar ratio of malonic acid, imidazole, and boric acid), pH 7.5, containing 25% v/v PEG 1500 and 5% v/v DMSO. Prior to crystallization compound solutions in DMSO were dried onto the wells of SwissCI 96-well plates. To achieve reproducible crystal growth seeding was used. Crystals appeared within a few hours and reached their final size after 2 -3 days. Crystals were manually harvested and flash cooled in liquid nitrogen for subsequent X-ray diffraction data collection.