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3 results for “Protein crystallography”
X-ray diffraction images recorded for Aumonier et al., (2022) Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature, IUCrJ
<p>The present repository contains diffraction images corresponding to 27 distinct datasets collected at room temperature on the ESRF beamline ID30A-3 using an Eiger X 4M detector.</p> <p>Datasets have been uploaded with their original names to maintain the metadata integrity. The two following tables match the original names with those attributed in the supplementary table S1 of Aumonier et al., IUCrJ (2022) (https://doi.org/10.1107/S2052252522009150).</p> <table> <tbody> <tr> <td> <p>Data set name on Zenodo</p> </td> <td> <p>X06_01</p> </td> <td> <p>X12_05</p> </td> <td> <p>X07_02_</p> </td> <td> <p>X06_08</p> </td> <td> <p>X14_06</p> </td> <td> <p>X13_03</p> </td> <td> <p>X08_06</p> </td> <td> <p>X11_05</p> </td> <td> <p>X13_05</p> </td> <td> <p>X06_02</p> </td> <td> <p>X11_01</p> </td> <td> <p>X08_01</p> </td> <td> <p>X14_01</p> </td> <td> <p>X13_01</p> </td> <td> <p>X06_03</p> </td> </tr> <tr> <td> <p>Data set in Aumonier et al. 2022</p> </td> <td> <p>Dark</p> </td> <td> <p>PS2</p> </td> <td> <p>PS2</p> </td> <td> <p>PS3</p> </td> <td> <p>PS4</p> </td> <td> <p>PS5</p> </td> <td> <p>PS6</p> </td> <td> <p>PS7</p> </td> <td> <p>R<sub>2”</sub></p> </td> <td> <p>R<sub>3”</sub></p> </td> <td> <p>R<sub>7”</sub></p> </td> <td> <p>R<sub>10”</sub></p> </td> <td> <p>R<sub>13”</sub></p> </td> <td> <p>R<sub>21”</sub></p> </td> <td> <p>R<sub>35”</sub></p> </td> </tr> </tbody> </table> <p> </p> <table> <tbody> <tr> <td> <p>Data set on Zenodo</p> </td> <td> <p>X08_02</p> </td> <td> <p>X11_02</p> </td> <td> <p>X12_02</p> </td> <td> <p>X14_02</p> </td> <td> <p>X13_04</p> </td> <td> <p>X13_02</p> </td> <td> <p>X12_06</p> </td> <td> <p>X06_09</p> </td> <td> <p>X09_04</p> </td> <td> <p>X12_04</p> </td> <td> <p>X06_07</p> </td> <td> <p>X13_07</p> </td> </tr> <tr> <td> <p>Data set in Aumonier et al. 2022</p> </td> <td> <p>R<sub>51”</sub></p> </td> <td> <p>R<sub>62”</sub></p> </td> <td> <p>R<sub>62”</sub></p> </td> <td> <p>R<sub>67”</sub></p> </td> <td> <p>R<sub>72”</sub></p> </td> <td> <p>R<sub>80”</sub></p> </td> <td> <p>R<sub>90”</sub></p> </td> <td> <p>R<sub>130”</sub></p> </td> <td> <p>R<sub>166”</sub></p> </td> <td> <p>R<sub>258”</sub></p> </td> <td> <p>R<sub>630”</sub></p> </td> <td> <p>R<sub>1620”</sub></p> </td> </tr> </tbody> </table> <p>One dataset consists of a master file, four data files and two metadata files.</p>
Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM
<p>This respository corresponds to the following paper: Wankowicz et al. Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM (2024). These are the qFit models. MTZ and deposited models cna be downloaded from the PDB. </p>
Body temperature protein X-ray crystallography at 37°C: A rhenium protein complex seeking a physiological condition structure: Raw Diffraction Images (112 week soak) Zenodo
<p>The labratory dataset of the raw diffraction images obtained after 112 weeks of soaking in the mother liquor and collected at a wavelength of 1.54 Å, illustrating the covalent coordination of the rhenium(I) tricarbonyl fragment to the His and Asp amino acid residues as well as other similarities when comparing the 37°C data set to 100K data set as described in the publication titled "Body temperature protein X-ray crystallography at 37°C: A rhenium protein complex seeking a physiological condition structure", written by Jacobs, Helliwell & Brink,<em> ChemComm</em>, 2024.</p> <p>The raw diffraction images for the labratory data sets are made available at the Zenodo research data archive, as specified in the publication.</p>
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