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Se-MAG is a convenient additive for experimental phasing and structure determination of membrane proteins crystallised by the lipid cubic phase (in meso) method
Boland, C., Huang, C. Y., Shanker Kaki, S., Wang, M., Olieric, V., & Caffrey, M. (2023). Se-MAG is a convenient additive for experimental phasing and structure determination of membrane proteins crystallised by the lipid cubic phase (in meso) method. Crystals, 13(9), 1402 (20 pp.). https://doi.org/10.3390/cryst13091402
SDU - software for high-throughput automated data collection at the Swiss Light Source
Smith, K. M. L., Panepucci, E., Kaminski, J. W., Aumonier, S., Huang, C. Y., Eris, D., … Wojdyla, J. A. (2023). SDU - software for high-throughput automated data collection at the Swiss Light Source. Journal of Synchrotron Radiation, 30, 538-545. https://doi.org/10.1107/S1600577523002631
Fast fragment and compound screening pipeline at the Swiss Light Source
Stegmann, D. P., Steuber, J., Fritz, G., Wojdyla, J. A., & Sharpe, M. E. (2023). Fast fragment and compound screening pipeline at the Swiss Light Source. Methods in enzymology: Vol. 690. (pp. 235-284). https://doi.org/10.1016/bs.mie.2023.08.005
Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation
Botte, M., Ni, D., Schenck, S., Zimmermann, I., Chami, M., Bocquet, N., … Hennig, M. (2022). Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation. Nature Communications, 13(1), 1826 (10 pp.). https://doi.org/10.1038/s41467-022-29459-2
<em>In vivo</em> photocontrol of microtubule dynamics and integrity, migration and mitosis, by the potent GFP-imaging-compatible photoswitchable reagents SBTubA4P and SBTub2M
Gao, L., Meiring, J. C. M., Varady, A., Ruider, I. E., Heise, C., Wranik, M., … Thorn-Seshold, O. (2022). In vivo photocontrol of microtubule dynamics and integrity, migration and mitosis, by the potent GFP-imaging-compatible photoswitchable reagents SBTubA4P and SBTub2M. Journal of the American Chemical Society, 144(12), 5614-5628. https://doi.org/10.1021/jacs.2c01020
Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography
Huang, C. Y., Aumonier, S., Engilberge, S., Eris, D., Smith, K. M. L., Leonarski, F., … Wang, M. (2022). Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 78, 964-974. https://doi.org/10.1107/S205979832200612X
Crystal structure of the pheromone E<em>r</em>-13 from the ciliate <em>Euplotes raikovi</em>, with implications for a protein-protein association model in pheromone/receptor interactions
Pedrini, B., Finke, A. D., Marsh, M., Luporini, P., Vallesi, A., & Alimenti, C. (2022). Crystal structure of the pheromone Er-13 from the ciliate Euplotes raikovi, with implications for a protein-protein association model in pheromone/receptor interactions. Journal of Structural Biology, 214(1), 107812 (10 pp.). https://doi.org/10.1016/j.jsb.2021.107812
A multispecific anti-CD40 DARPin construct induces tumor-selective CD40 activation and tumor regression
Rigamonti, N., Veitonmäki, N., Domke, C., Barsin, S., Jetzer, S., Abdelmotaleb, O., … Trail, P. A. (2022). A multispecific anti-CD40 DARPin construct induces tumor-selective CD40 activation and tumor regression. Cancer Immunology Research, 10(5), 626-640. https://doi.org/10.1158/2326-6066.CIR-21-0553
Novel fragment-derived colchicine-site binders as microtubule-destabilizing agents
de la Roche, N. M., Mühlethaler, T., Di Martino, R. M. C., Ortega, J. A., Gioia, D., Roy, B., … Cavalli, A. (2022). Novel fragment-derived colchicine-site binders as microtubule-destabilizing agents. European Journal of Medicinal Chemistry, 241, 114614 (12 pp.). https://doi.org/10.1016/j.ejmech.2022.114614
Optimizing the growth of endothiapepsin crystals for serial crystallography experiments
Beale, J. H., & Marsh, M. E. (2021). Optimizing the growth of endothiapepsin crystals for serial crystallography experiments. Journal of Visualized Experiments, 168, e61896 (30 pp.). https://doi.org/10.3791/61896
Versatile microporous polymer-based supports for serial macromolecular crystallography
Martiel, I., Beale, J. H., Karpik, A., Huang, C. Y., Vera, L., Olieric, N., … Padeste, C. (2021). Versatile microporous polymer-based supports for serial macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 77(9), 1153-1167. https://doi.org/10.1107/S2059798321007324
<em>In situ</em> crystallography as an emerging method for structure solution of membrane proteins: the case of CCR2A
Cheng, R., Huang, C. Y., Hennig, M., Nar, H., & Schnapp, G. (2020). In situ crystallography as an emerging method for structure solution of membrane proteins: the case of CCR2A. FEBS Journal, 287(5), 866-873. https://doi.org/10.1111/febs.15098
In meso in situ serial X-Ray crystallography (IMISX): a protocol for membrane protein structure determination at the Swiss Light Source
Huang, C. Y., Olieric, V., Caffrey, M., & Wang, M. (2020). In meso in situ serial X-Ray crystallography (IMISX): a protocol for membrane protein structure determination at the Swiss Light Source. In C. Perez & T. Maier (Eds.), Methods in molecular biology: Vol. 2127. Expression, purification, and structural biology of membrane proteins (pp. 293-319). https://doi.org/10.1007/978-1-0716-0373-4_20
Distinctive structural properties of THB11, a pentacoordinate &lt;em&gt;Chlamydomonas reinhardtii&lt;/em&gt; truncated hemoglobin with N- and C-terminal extensions
Huwald, D., Duda, S., Gasper, R., Olieric, V., Hofmann, E., & Hemschemeier, A. (2020). Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions. Journal of Biological Inorganic Chemistry, 25, 267-283. https://doi.org/10.1007/s00775-020-01759-2
Serial femtosecond <em>zero dose</em> crystallography captures a water-free distal heme site in a dye‐decolourising peroxidase to reveal a catalytic role for an arginine in Fe<sup>IV</sup>=O formation
Lučić, M., Svistunenko, D. A., Wilson, M. T., Chaplin, A. K., Davy, B., Ebrahim, A., … Worrall, J. A. R. (2020). Serial femtosecond zero dose crystallography captures a water-free distal heme site in a dye‐decolourising peroxidase to reveal a catalytic role for an arginine in FeIV=O formation. Angewandte Chemie International Edition, 59(48), 21656-21662. https://doi.org/10.1002/anie.202008622
The TELL automatic sample changer for macromolecular crystallography
Martiel, I., Buntschu, D., Meier, N., Gobbo, A., Panepucci, E., Schneider, R., … Wang, M. (2020). The TELL automatic sample changer for macromolecular crystallography. Journal of Synchrotron Radiation, 27, 860-863. https://doi.org/10.1107/S1600577520002416
A nitric oxide-binding heterodimeric cytochrome <em>c</em> complex from the anammox bacterium <em>Kuenenia stuttgartiensis </em>binds to hydrazine synthase
Akram, M., Reimann, J., Dietl, A., Menzel, A., Versantvoort, W., Kartal, B., … Barends, T. R. M. (2019). A nitric oxide-binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase. Journal of Biological Chemistry, 294(45), 16712-16728. https://doi.org/10.1074/jbc.RA119.008788
Crystal structure of CC chemokine receptor 2A in complex with an orthosteric antagonist provides insights for the design of selective antagonists
Apel, A. K., Cheng, R. K. Y., Tautermann, C. S., Brauchle, M., Huang, C. Y., Pautsch, A., … Schnapp, G. (2019). Crystal structure of CC chemokine receptor 2A in complex with an orthosteric antagonist provides insights for the design of selective antagonists. Structure, 27(3), 427-438.e5. https://doi.org/10.1016/j.str.2018.10.027
Automated data collection and real-time data analysis suite for serial synchrotron crystallography
Basu, S., Kaminski, J. W., Panepucci, E., Huang, C. Y., Warshamanage, R., Wang, M., & Wojdyla, J. A. (2019). Automated data collection and real-time data analysis suite for serial synchrotron crystallography. Journal of Synchrotron Radiation, 26(1), 244-252. https://doi.org/10.1107/S1600577518016570
Alternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria
Żyła, D. S., Prota, A. E., Capitani, G., & Glockshuber, R. (2019). Alternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria. Journal of Biological Chemistry, 294(27), 10553-10563. https://doi.org/10.1074/jbc.RA119.008610
 

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