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A lathe system for micrometre-sized cylindrical sample preparation at room and cryogenic temperatures
Holler, M., Ihli, J., Tsai, E. H. R., Nudelman, F., Verezhak, M., van de Berg, W. D. J., & Shahmoradian, S. H. (2020). A lathe system for micrometre-sized cylindrical sample preparation at room and cryogenic temperatures. Journal of Synchrotron Radiation, 27(2), 472-476. https://doi.org/10.1107/S1600577519017028
Holography and coherent diffraction imaging with low-(30-250 eV) and high-(80-300 keV) energy electrons: history, principles, and recent trends
Latychevskaia, T. (2020). Holography and coherent diffraction imaging with low-(30-250 eV) and high-(80-300 keV) energy electrons: history, principles, and recent trends. Materials, 13(14), 3089 (36 pp.). https://doi.org/10.3390/ma13143089
A lipocalin mediates unidirectional heme biomineralization in malaria parasites
Matz, J. M., Drepper, B., Blum, T. B., van Genderen, E., Burrell, A., Martin, P., Stach, T., Collinson, L. M., Abrahams, J. P., Matuschewski, K., & Blackman, M. J. (2020). A lipocalin mediates unidirectional heme biomineralization in malaria parasites. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(28), 16546-16556. https://doi.org/10.1073/pnas.2001153117
GPCR solubilization and quality control
Miljus, T., Sykes, D. A., Harwood, C. R., Vuckovic, Z., & Veprintsev, D. B. (2020). GPCR solubilization and quality control. In C. Perez & T. Maier (Eds.), Methods in molecular biology: Vol. 2127. Expression, purification, and structural biology of membrane proteins (pp. 105-127). https://doi.org/10.1007/978-1-0716-0373-4_8
Antimicrobial peptide mimetics based on a diphenylacetylene scaffold: synthesis, conformational analysis, and activity
Peacock, H., Henriques, S. T., Benfield, A. H., Elliott, A. G., Luo, J., Luccarelli, J., Nagano, M., Craik, D. J., & Hamilton, A. D. (2020). Antimicrobial peptide mimetics based on a diphenylacetylene scaffold: synthesis, conformational analysis, and activity. ChemMedChem. https://doi.org/10.1002/cmdc.202000474
The structure and symmetry of the radial spoke protein complex in <em>Chlamydomonas </em>flagella
Poghosyan, E., Iacovache, I., Faltova, L., Leitner, A., Yang, P., Diener, D. R., Aebersold, R., Zuber, B., & Ishikawa, T. (2020). The structure and symmetry of the radial spoke protein complex in Chlamydomonas flagella. Journal of Cell Science, 133(16), jcs245233. https://doi.org/10.1242/jcs.245233
Femtosecond-to-millisecond structural changes in a light-driven sodium pump
Skopintsev, P., Ehrenberg, D., Weinert, T., James, D., Kar, R. K., Johnson, P. J. M., Ozerov, D., Furrer, A., Martiel, I., Dworkowski, F., Nass, K., Knopp, G., Cirelli, C., Arrell, C., Gashi, D., Mous, S., Wranik, M., Gruhl, T., Kekilli, D., … Standfuss, J. (2020). Femtosecond-to-millisecond structural changes in a light-driven sodium pump. Nature. https://doi.org/10.1038/s41586-020-2307-8
New insights into arrestin recruitment to GPCRs
Spillmann, M., Thurner, L., Romantini, N., Zimmermann, M., Meger, B., Behe, M., Waldhoer, M., Schertler, G. F. X., & Berger, P. (2020). New insights into arrestin recruitment to GPCRs. International Journal of Molecular Sciences, 21(14), 4949 (14 pp.). https://doi.org/10.3390/ijms21144949
Sub-pixel electron detection using a convolutional neural network
van Schayck, J. P., van Genderen, E., Maddox, E., Roussel, L., Boulanger, H., Fröjdh, E., Abrahams, J. P., Peters, P. J., & Ravelli, R. B. G. (2020). Sub-pixel electron detection using a convolutional neural network. Ultramicroscopy, 218, 113091 (10 pp.). https://doi.org/10.1016/j.ultramic.2020.113091
The wild-type flagellar filament of the Firmicute <em>Kurthia </em>at 2.8 Å resolution <em>in vivo</em>
Blum, T. B., Filippidou, S., Fatton, M., Junier, P., & Abrahams, J. P. (2019). The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo. Scientific Reports, 9(1), 14948 (8 pp.). https://doi.org/10.1038/s41598-019-51440-1
Reducing dynamical electron scattering reveals hydrogen atoms
Clabbers, M. T. B., Gruene, T., van Genderen, E., & Abrahams, J. P. (2019). Reducing dynamical electron scattering reveals hydrogen atoms. Acta Crystallographica Section A: Foundations and Advances, 75(1), 82-93. https://doi.org/10.1107/S2053273318013918
3D electron diffraction: the nanocrystallography revolution
Gemmi, M., Mugnaioli, E., Gorelik, T. E., Kolb, U., Palatinus, L., Boullay, P., Hovmöller, S., & Abrahams, J. P. (2019). 3D electron diffraction: the nanocrystallography revolution. ACS Central Science, 5(8), 1315-1329. https://doi.org/10.1021/acscentsci.9b00394
Structure and transformation of bacteriophage A511 baseplate and tail upon infection of <em>Listeria </em>cells
Guerrero-Ferreira, R. C., Hupfeld, M., Nazarov, S., Taylor, N. M. I., Shneider, M. M., Obbineni, J. M., Loessner, M. J., Ishikawa, T., Klumpp, J., & Leiman, P. G. (2019). Structure and transformation of bacteriophage A511 baseplate and tail upon infection of Listeria cells. EMBO Journal, 38(3), e99455 (20 pp.). https://doi.org/10.15252/embj.201899455
Arrestin-1 engineering facilitates complex stabilization with native rhodopsin
Haider, R. S., Wilhelm, F., Rizk, A., Mutt, E., Deupi, X., Peterhans, C., Mühle, J., Berger, P., Schertler, G. F. X., Standfuss, J., & Ostermaier, M. K. (2019). Arrestin-1 engineering facilitates complex stabilization with native rhodopsin. Scientific Reports, 9(1), 439 (13 pp.). https://doi.org/10.1038/s41598-018-36881-4
Design guidelines for an electron diffractometer for structural chemistry and structural biology
Heidler, J., Pantelic, R., Wennmacher, J. T. C., Zaubitzer, C., Fecteau-Lefebvre, A., Goldie, K. N., Müller, E., Holstein, J. J., van Genderen, E., De Carlo, S., & Gruene, T. (2019). Design guidelines for an electron diffractometer for structural chemistry and structural biology. Acta Crystallographica Section D: Structural Biology, 75(5), 458-466. https://doi.org/10.1107/S2059798319003942
Three-dimensional imaging of integrated circuits with macro- to nanoscale zoom
Holler, M., Odstrcil, M., Guizar-Sicairos, M., Lebugle, M., Müller, E., Finizio, S., Tinti, G., David, C., Zusman, J., Unglaub, W., Bunk, O., Raabe, J., Levi, A. F. J., & Aeppli, G. (2019). Three-dimensional imaging of integrated circuits with macro- to nanoscale zoom. Nature Electronics, 2, 464-470. https://doi.org/10.1038/s41928-019-0309-z
Effect of template type on the <em>Trametes versicolor</em> laccase-catalyzed oligomerization of the aniline dimer <em>p</em>-aminodiphenylamine (PADPA)
Kashima, K., Fujisaki, T., Serrano-Luginbühl, S., Kissner, R., Janošević Ležaić, A., Bajuk-Bogdanović, D., Ćirić-Marjanović, G., Busato, S., Ishikawa, T., & Walde, P. (2019). Effect of template type on the Trametes versicolor laccase-catalyzed oligomerization of the aniline dimer p-aminodiphenylamine (PADPA). ACS Omega, 4(2), 2931-2947. https://doi.org/10.1021/acsomega.8b03441
Seamless insert-plasmid assembly at sub-terminal homologous sequences
Krebs, A. S., Bierig, T., Collu, G., & Benoit, R. M. (2019). Seamless insert-plasmid assembly at sub-terminal homologous sequences. Plasmid, 106, 102445 (9 pp.). https://doi.org/10.1016/j.plasmid.2019.102445
Ferroelectric self-poling in GeTe films and crystals
Kriegner, D., Springholz, G., Richter, C., Pilet, N., Müller, E., Capron, M., Berger, H., Holý, V., Dil, J. H., & Krempaský, J. (2019). Ferroelectric self-poling in GeTe films and crystals. Crystals, 9(7), 335 (15 pp.). https://doi.org/10.3390/cryst9070335
Inelastic scattering and solvent scattering reduce dynamical diffraction in biological crystals
Latychevskaia, T., & Abrahams, J. P. (2019). Inelastic scattering and solvent scattering reduce dynamical diffraction in biological crystals. Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 75, 523-531. https://doi.org/10.1107/S2052520619009661
 

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