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Mohammed, Inayathulla, Schmitz, Kai A., Schenck, Niko, Balasopoulos, Dimitrios, Topitsch, Annika, Maier, Timm, & . (2022). Catalytic cycling of human mitochondrial Lon protease. Structure, 30(9), 1254–1268. https://doi.org/10.1016/j.str.2022.06.006
Mohammed, Inayathulla, Schmitz, Kai A., Schenck, Niko, Balasopoulos, Dimitrios, Topitsch, Annika, Maier, Timm, & . (2022). Catalytic cycling of human mitochondrial Lon protease. Structure, 30(9), 1254–1268. https://doi.org/10.1016/j.str.2022.06.006
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Ling, Wai Li, & . (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica Section D: Structural Biology, 77(Pt 1), 75–85. https://doi.org/10.1107/s2059798320014540
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Ling, Wai Li, & . (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica Section D: Structural Biology, 77(Pt 1), 75–85. https://doi.org/10.1107/s2059798320014540
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Li Ling, Wai, & . (2020). Statistically correcting dynamical electron scattering improves refinement of protein nanocrystals, including charge refinement of coordinated metals. bioRxiv. https://doi.org/10.1101/2020.07.08.191049
Blum, Thorsten B., Housset, Dominique, Clabbers, Max T. B., van Genderen, Eric, Bacia-Verloop, Maria, Zander, Ulrich, McCarthy, Andrew A., Schoehn, Guy, Li Ling, Wai, & . (2020). Statistically correcting dynamical electron scattering improves refinement of protein nanocrystals, including charge refinement of coordinated metals. bioRxiv. https://doi.org/10.1101/2020.07.08.191049
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy, , Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional haem biomineralization in malaria parasites. In bioRxiv. bioRxiv. https://doi.org/10.1101/2020.02.18.954289
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy, , Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional haem biomineralization in malaria parasites. In bioRxiv. bioRxiv. https://doi.org/10.1101/2020.02.18.954289
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy M., , Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional heme biomineralization in malaria parasites. Proceedings of the National Academy of Sciences of the United States of America, 117(28), 16546–16556. https://doi.org/10.1073/pnas.2001153117
Matz, Joachim M., Drepper, Benjamin, Blum, Thorsten B., van Genderen, Eric, Burrell, Alana, Martin, Peer, Stach, Thomas, Collinson, Lucy M., , Matuschewski, Kai, & Blackman, Michael J. (2020). A lipocalin mediates unidirectional heme biomineralization in malaria parasites. Proceedings of the National Academy of Sciences of the United States of America, 117(28), 16546–16556. https://doi.org/10.1073/pnas.2001153117
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Blum, Thorsten B., Zuo, Xiaobing, Bazrafshan, Alisina, Siaw, Hew Ming Helen, McCanna, Arthur, Dyer, R. Brian, Salaita, Khalid, , & Conticello, Vincent P. (2020). Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets. Journal of the American Chemical Society, 142(47), 19956–19968. https://doi.org/10.1021/jacs.0c08174
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Blum, Thorsten B., Zuo, Xiaobing, Bazrafshan, Alisina, Siaw, Hew Ming Helen, McCanna, Arthur, Dyer, R. Brian, Salaita, Khalid, , & Conticello, Vincent P. (2020). Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets. Journal of the American Chemical Society, 142(47), 19956–19968. https://doi.org/10.1021/jacs.0c08174
Thakkar, Pooja, Guzenko, Vitaliy A., Lu, Peng-Han, Dunin-Borkowski, Rafal E., , & Tsujino, Soichiro. (2020). Fabrication of low aspect ratio three-element Boersch phase shifters for voltage-controlled three electron beam interference. Journal of Applied Physics, 128(13), 134502. https://doi.org/10.1063/5.0020383
Thakkar, Pooja, Guzenko, Vitaliy A., Lu, Peng-Han, Dunin-Borkowski, Rafal E., , & Tsujino, Soichiro. (2020). Fabrication of low aspect ratio three-element Boersch phase shifters for voltage-controlled three electron beam interference. Journal of Applied Physics, 128(13), 134502. https://doi.org/10.1063/5.0020383
van Schayck, J. Paul, van Genderen, Eric, Maddox, Erik, Roussel, Lucas, Boulanger, Hugo, Fröjdh, Erik, , Peters, Peter J., & Ravelli, Raimond B. G. (2020). Sub-pixel electron detection using a convolutional neural network. Ultramicroscopy, 218, 113091. https://doi.org/10.1016/j.ultramic.2020.113091
van Schayck, J. Paul, van Genderen, Eric, Maddox, Erik, Roussel, Lucas, Boulanger, Hugo, Fröjdh, Erik, , Peters, Peter J., & Ravelli, Raimond B. G. (2020). Sub-pixel electron detection using a convolutional neural network. Ultramicroscopy, 218, 113091. https://doi.org/10.1016/j.ultramic.2020.113091
Xiao, Xiansha, Elsayed, Somayah S., Wu, Changsheng, van der Heul, Helga U., Metsä-Ketelä, Mikko, Du, Chao, Prota, Andrea E., Chen, Chun-Chi, Liu, Weidong, Guo, Rey-Ting, , & van Wezel, Gilles P. (2020). Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway. ACS Chemical Biology, 15(9), 2529–2538. https://doi.org/10.1021/acschembio.0c00564
Xiao, Xiansha, Elsayed, Somayah S., Wu, Changsheng, van der Heul, Helga U., Metsä-Ketelä, Mikko, Du, Chao, Prota, Andrea E., Chen, Chun-Chi, Liu, Weidong, Guo, Rey-Ting, , & van Wezel, Gilles P. (2020). Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway. ACS Chemical Biology, 15(9), 2529–2538. https://doi.org/10.1021/acschembio.0c00564
Zhang, Zhenzhen, Wen, Kai, Zhang, Chao, Laroche, Fabrice, Wang, Zhenglong, Zhou, Qiang, Liu, Zunfeng, , & Zhou, Xiang. (2020). Extracellular Nanovesicle Enhanced Gene Transfection Using Polyethyleneimine in HEK293T Cells and Zebrafish Embryos. Frontiers in Bioengineering and Biotechnology, 8, 448. https://doi.org/10.3389/fbioe.2020.00448
Zhang, Zhenzhen, Wen, Kai, Zhang, Chao, Laroche, Fabrice, Wang, Zhenglong, Zhou, Qiang, Liu, Zunfeng, , & Zhou, Xiang. (2020). Extracellular Nanovesicle Enhanced Gene Transfection Using Polyethyleneimine in HEK293T Cells and Zebrafish Embryos. Frontiers in Bioengineering and Biotechnology, 8, 448. https://doi.org/10.3389/fbioe.2020.00448
Blum, T. B., & (2019). 6T17: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia. Worldwide Protein Data Bank, 6T17. https://doi.org/10.2210/pdb6t17/pdb
Blum, T. B., & (2019). 6T17: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia. Worldwide Protein Data Bank, 6T17. https://doi.org/10.2210/pdb6t17/pdb
Blum, Thorsten B., Filippidou, Sevasti, Fatton, Mathilda, Junier, Pilar, & . (2019). The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo. Scientific Reports, 9(1), 14948. https://doi.org/10.1038/s41598-019-51440-1
Blum, Thorsten B., Filippidou, Sevasti, Fatton, Mathilda, Junier, Pilar, & . (2019). The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo. Scientific Reports, 9(1), 14948. https://doi.org/10.1038/s41598-019-51440-1
Clabbers, Max T. B., Gruene, Tim, van Genderen, Eric, & . (2019). Reducing dynamical electron scattering reveals hydrogen atoms. Acta Crystallographica. Section A, Foundations and Advances, 75(Pt 1), 82–93. https://doi.org/10.1107/s2053273318013918
Clabbers, Max T. B., Gruene, Tim, van Genderen, Eric, & . (2019). Reducing dynamical electron scattering reveals hydrogen atoms. Acta Crystallographica. Section A, Foundations and Advances, 75(Pt 1), 82–93. https://doi.org/10.1107/s2053273318013918
Gemmi, Mauro, Mugnaioli, Enrico, Gorelik, Tatiana E., Kolb, Ute, Palatinus, Lukas, Boullay, Philippe, Hovmöller, Sven, & . (2019). 3D Electron Diffraction: The Nanocrystallography Revolution. ACS Central Science, 5(8), 1315–1329. https://doi.org/10.1021/acscentsci.9b00394
Gemmi, Mauro, Mugnaioli, Enrico, Gorelik, Tatiana E., Kolb, Ute, Palatinus, Lukas, Boullay, Philippe, Hovmöller, Sven, & . (2019). 3D Electron Diffraction: The Nanocrystallography Revolution. ACS Central Science, 5(8), 1315–1329. https://doi.org/10.1021/acscentsci.9b00394
Latychevskaia, Tatiana, & . (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
Latychevskaia, Tatiana, & . (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
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Zuo, Xiaobing, Bazrafshan, Alisina, Blum, Thorsten, Hughes, Spencer, Salaita, Khalid, , & Conticello, Vincent P. (2019). 2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks. Angewandte Chemie (International Ed. In English), 58(38), 13507–13512. https://doi.org/10.1002/anie.201906214
Merg, Andrea D., Touponse, Gavin, van Genderen, Eric, Zuo, Xiaobing, Bazrafshan, Alisina, Blum, Thorsten, Hughes, Spencer, Salaita, Khalid, , & Conticello, Vincent P. (2019). 2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks. Angewandte Chemie (International Ed. In English), 58(38), 13507–13512. https://doi.org/10.1002/anie.201906214
Merg, Andrea D., van Genderen, Eric, Bazrafshan, Alisina, Su, Hanquan, Zuo, Xiaobing, Touponse, Gavin, Blum, Thorsten B., Salaita, Khalid, , & Conticello, Vincent P. (2019). Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core-Shell Nanostructures. Journal of the American Chemical Society, 141(51), 20107–20117. https://doi.org/10.1021/jacs.9b09335
Merg, Andrea D., van Genderen, Eric, Bazrafshan, Alisina, Su, Hanquan, Zuo, Xiaobing, Touponse, Gavin, Blum, Thorsten B., Salaita, Khalid, , & Conticello, Vincent P. (2019). Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core-Shell Nanostructures. Journal of the American Chemical Society, 141(51), 20107–20117. https://doi.org/10.1021/jacs.9b09335
Moradi, Mina, Opara, Nadia L., Tulli, Ludovico G., Wäckerlin, Christian, Dalgarno, Scott J., Teat, Simon J., Baljozovic, Milos, Popova, Olha, van Genderen, Eric, Kleibert, Armin, Stahlberg, Henning, , Padeste, Celestino, Corvini, Philippe F.-X., Jung, Thomas A., & Shahgaldian, Patrick. (2019). Supramolecular architectures of molecularly thin yet robust free-standing layers. Science Advances, 5(2), eaav4489. https://doi.org/10.1126/sciadv.aav4489
Moradi, Mina, Opara, Nadia L., Tulli, Ludovico G., Wäckerlin, Christian, Dalgarno, Scott J., Teat, Simon J., Baljozovic, Milos, Popova, Olha, van Genderen, Eric, Kleibert, Armin, Stahlberg, Henning, , Padeste, Celestino, Corvini, Philippe F.-X., Jung, Thomas A., & Shahgaldian, Patrick. (2019). Supramolecular architectures of molecularly thin yet robust free-standing layers. Science Advances, 5(2), eaav4489. https://doi.org/10.1126/sciadv.aav4489
Wallin, Cecilia, Hiruma, Yoshitaka, Warmlander, Sebastian, Huvent, Isabelle, Jarvet, Juri, , Graslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2019). The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-beta (A beta) Peptide (Patent No. 3, Supplement 1). Biophysical Journal, 116(3, Supplement 1), Article 3, Supplement 1. https://doi.org/10.1016/j.bpj.2018.11.1657
Wallin, Cecilia, Hiruma, Yoshitaka, Warmlander, Sebastian, Huvent, Isabelle, Jarvet, Juri, , Graslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2019). The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-beta (A beta) Peptide (Patent No. 3, Supplement 1). Biophysical Journal, 116(3, Supplement 1), Article 3, Supplement 1. https://doi.org/10.1016/j.bpj.2018.11.1657
, Clabbers, Max, van Genderen, Eric, & Blum, Thorsten. (2018). Electron tomography of radiation sensitive 3D nano-crystals in imaging and diffraction mode [International Union of Crystallography]. Acta Crystallographica A-Foundation and Advances, 74, E83. https://doi.org/10.1107/s205327331809397x
, Clabbers, Max, van Genderen, Eric, & Blum, Thorsten. (2018). Electron tomography of radiation sensitive 3D nano-crystals in imaging and diffraction mode [International Union of Crystallography]. Acta Crystallographica A-Foundation and Advances, 74, E83. https://doi.org/10.1107/s205327331809397x
Clabbers, Max, Gruene, Tim, van Genderen, Eric, & . (2018). Experimental and computational reduction of dynamical electron scattering allows visualizing individual hydrogen atoms [International Union of Crystallography]. Acta Crystallographica A-Foundation and Advances, 74, E426. https://doi.org/10.1107/s2053273318088770
Clabbers, Max, Gruene, Tim, van Genderen, Eric, & . (2018). Experimental and computational reduction of dynamical electron scattering allows visualizing individual hydrogen atoms [International Union of Crystallography]. Acta Crystallographica A-Foundation and Advances, 74, E426. https://doi.org/10.1107/s2053273318088770
Clabbers, Max T. B., & . (2018). Electron diffraction and three-dimensional crystallography for structural biology. Crystallography Reviews, 24(3), 176–204. https://doi.org/10.1080/0889311x.2018.1446427
Clabbers, Max T. B., & . (2018). Electron diffraction and three-dimensional crystallography for structural biology. Crystallography Reviews, 24(3), 176–204. https://doi.org/10.1080/0889311x.2018.1446427
Clabbers, Max T. B., Gruene, Tim, Parkhurst, James M., , & Waterman, David G. (2018). Electron diffraction data processing with DIALS. Acta Crystallographica. Section D, Structural Biology, 74(Pt 6), 506–518. https://doi.org/10.1107/s2059798318007726
Clabbers, Max T. B., Gruene, Tim, Parkhurst, James M., , & Waterman, David G. (2018). Electron diffraction data processing with DIALS. Acta Crystallographica. Section D, Structural Biology, 74(Pt 6), 506–518. https://doi.org/10.1107/s2059798318007726
Thomas, Brijith, Dubey, Rajeev K., Clabbers, Max T. B., Gupta, Karthick Babu Sai Sankar, van Genderen, Eric, Jager, Wolter F., , Sudholter, Ernst J. R., & de Groot, Huub J. M. (2018). A Molecular Level Approach To Elucidate the Supramolecular Packing of Light-Harvesting Antenna Systems. Chemistry (Weinheim an Der Bergstrasse, Germany), 24(56), 14989–14993. https://doi.org/10.1002/chem.201802288
Thomas, Brijith, Dubey, Rajeev K., Clabbers, Max T. B., Gupta, Karthick Babu Sai Sankar, van Genderen, Eric, Jager, Wolter F., , Sudholter, Ernst J. R., & de Groot, Huub J. M. (2018). A Molecular Level Approach To Elucidate the Supramolecular Packing of Light-Harvesting Antenna Systems. Chemistry (Weinheim an Der Bergstrasse, Germany), 24(56), 14989–14993. https://doi.org/10.1002/chem.201802288
Tinti, Gemma, Fröjdh, Erik, van Genderen, Eric, Gruene, Tim, Schmitt, Bernd, de Winter, D. A. Matthijs, Weckhuysen, Bert M., & . (2018). Electron crystallography with the EIGER detector. IUCrJ, 5(Pt 2), 190–199. https://doi.org/10.1107/s2052252518000945
Tinti, Gemma, Fröjdh, Erik, van Genderen, Eric, Gruene, Tim, Schmitt, Bernd, de Winter, D. A. Matthijs, Weckhuysen, Bert M., & . (2018). Electron crystallography with the EIGER detector. IUCrJ, 5(Pt 2), 190–199. https://doi.org/10.1107/s2052252518000945
Tinti, G., Frojdh, E., Van Genderen, E., Gruene, T., Schmitt, B., De Winter, D. A. M., Weckhuysen, B. M., & (2018). CCDC 1817054: Experimental Crystal Structure Determination. Cambridge Structural Database, 1817054. https://doi.org/10.5517/ccdc.csd.cc1yzsnc
Tinti, G., Frojdh, E., Van Genderen, E., Gruene, T., Schmitt, B., De Winter, D. A. M., Weckhuysen, B. M., & (2018). CCDC 1817054: Experimental Crystal Structure Determination. Cambridge Structural Database, 1817054. https://doi.org/10.5517/ccdc.csd.cc1yzsnc
Wallin, Cecilia, Hiruma, Yoshitaka, Wärmländer, Sebastian K. T. S., Huvent, Isabelle, Jarvet, Jüri, , Gräslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2018). The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage. Journal of the American Chemical Society, 8138–8146. https://doi.org/10.1021/jacs.7b13623
Wallin, Cecilia, Hiruma, Yoshitaka, Wärmländer, Sebastian K. T. S., Huvent, Isabelle, Jarvet, Jüri, , Gräslund, Astrid, Lippens, Guy, & Luo, Jinghui. (2018). The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage. Journal of the American Chemical Society, 8138–8146. https://doi.org/10.1021/jacs.7b13623
Clabbers, Max T. B., van Genderen, Eric, Wan, Wei, Wiegers, Emiel L., Gruene, Tim, & . (2017). Protein structure determination by electron diffraction using a single three-dimensional nanocrystal. Acta Crystallographica. Section D, Structural Biology, 73(Pt 9), 738–748. https://doi.org/10.1107/s2059798317010348
Clabbers, Max T. B., van Genderen, Eric, Wan, Wei, Wiegers, Emiel L., Gruene, Tim, & . (2017). Protein structure determination by electron diffraction using a single three-dimensional nanocrystal. Acta Crystallographica. Section D, Structural Biology, 73(Pt 9), 738–748. https://doi.org/10.1107/s2059798317010348
Matheson, John, Moldovan, G., Kirkland, Angus, Allinson, Nigel, & . (2017). Testing and Comparison of Imaging Detectors for Electrons in the Energy Range 10-20 keV. Journal of Instrumentation, 12(11), C11016. https://doi.org/10.1088/1748-0221/12/11/c11016
Matheson, John, Moldovan, G., Kirkland, Angus, Allinson, Nigel, & . (2017). Testing and Comparison of Imaging Detectors for Electrons in the Energy Range 10-20 keV. Journal of Instrumentation, 12(11), C11016. https://doi.org/10.1088/1748-0221/12/11/c11016
Nederlof, Igor, van Genderen, Eric, Clabbers, Maddox E., & . (2017). Electron Crystallography of Protein Nano-Crystals. Acta Crystallographica Section A: Foundations and Advances, A73, a297–a298. https://doi.org/10.1107/s0108767317097082
Nederlof, Igor, van Genderen, Eric, Clabbers, Maddox E., & . (2017). Electron Crystallography of Protein Nano-Crystals. Acta Crystallographica Section A: Foundations and Advances, A73, a297–a298. https://doi.org/10.1107/s0108767317097082
Nikolopoulos, Stavros, Galanis, Athanasios S., Vallcorba, Oriol, Eggeman, Alex, Das, Partha Pratim, , Rauch, Edgar, Midgley, Paul, & Gemmi, Mauro. (2017). Random electron diffraction tomography for structure analysis of pharmaceuticals. Acta Crystallographica A-Foundation and Advances, 73, C980–C980. https://doi.org/10.1107/s2053273317085941
Nikolopoulos, Stavros, Galanis, Athanasios S., Vallcorba, Oriol, Eggeman, Alex, Das, Partha Pratim, , Rauch, Edgar, Midgley, Paul, & Gemmi, Mauro. (2017). Random electron diffraction tomography for structure analysis of pharmaceuticals. Acta Crystallographica A-Foundation and Advances, 73, C980–C980. https://doi.org/10.1107/s2053273317085941
Su, Jian, Wang, Hongyan, Wu, Kunkun, Liu, Zhongsheng, Yin, Qu, Wang, Run, Lv, Wei, Yin, Shougen, Liu, Zunfeng, & . (2017). Neutravidin-Mediated Extraction of Isolated Small Diameter Single Walled Carbon Nanotubes for Bio-Recognition. Journal of Nanoscience and Nanotechnology, 17(5), 3588–3596. https://doi.org/10.1166/jnn.2017.12860
Su, Jian, Wang, Hongyan, Wu, Kunkun, Liu, Zhongsheng, Yin, Qu, Wang, Run, Lv, Wei, Yin, Shougen, Liu, Zunfeng, & . (2017). Neutravidin-Mediated Extraction of Isolated Small Diameter Single Walled Carbon Nanotubes for Bio-Recognition. Journal of Nanoscience and Nanotechnology, 17(5), 3588–3596. https://doi.org/10.1166/jnn.2017.12860
Wang, Run, Boleij, Marissa, Yin, Qu, Galjart, Niels, Lin, Bencai, Yuan, Ningyi, Zhou, Xiang, Tan, Ming, Ding, Jianning, Liu, Zunfeng, & . (2017). Purification of Biotinylated Proteins Using Single Walled Carbon Nanotube-Streptavidin Complexes. Journal of Nanoscience and Nanotechnology, 17(2), 31–926. https://doi.org/10.1166/jnn.2017.12716
Wang, Run, Boleij, Marissa, Yin, Qu, Galjart, Niels, Lin, Bencai, Yuan, Ningyi, Zhou, Xiang, Tan, Ming, Ding, Jianning, Liu, Zunfeng, & . (2017). Purification of Biotinylated Proteins Using Single Walled Carbon Nanotube-Streptavidin Complexes. Journal of Nanoscience and Nanotechnology, 17(2), 31–926. https://doi.org/10.1166/jnn.2017.12716
Yin, Qu, Liu, Zunfeng, Laroche, Fabrice, Zhou, Xiang, Shao, Ningning, Lin, Bencai, Wang, Run, Yuan, Ningyi, Ding, Jianning, & . (2017). A Novel Capturing Method for Quantification of Extra-Cellular Nanovesicles. Journal of Nanoscience and Nanotechnology, 17(2), 908–913. https://doi.org/10.1166/jnn.2017.12631
Yin, Qu, Liu, Zunfeng, Laroche, Fabrice, Zhou, Xiang, Shao, Ningning, Lin, Bencai, Wang, Run, Yuan, Ningyi, Ding, Jianning, & . (2017). A Novel Capturing Method for Quantification of Extra-Cellular Nanovesicles. Journal of Nanoscience and Nanotechnology, 17(2), 908–913. https://doi.org/10.1166/jnn.2017.12631
. (2016). Electron nanodiffraction for structural biology. Acta Crystallographica A-Foundation and Advances, 72(a1), S6–S6. https://doi.org/10.1107/s2053273316099903
. (2016). Electron nanodiffraction for structural biology. Acta Crystallographica A-Foundation and Advances, 72(a1), S6–S6. https://doi.org/10.1107/s2053273316099903
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & . (2016). Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II. ACS Chemical Neuroscience, 7(3), 74–269. https://doi.org/10.1021/acschemneuro.5b00325
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & . (2016). Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II. ACS Chemical Neuroscience, 7(3), 74–269. https://doi.org/10.1021/acschemneuro.5b00325
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, & . (2016). Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis. Journal of Biological Chemistry, 292(5), 2046. https://doi.org/10.1074/jbc.r116.714576
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Tiiman, Ann, Luo, Jinghui, Wallin, Cecilia, Olsson, Lisa, Lindgren, Joel, Jarvet, Jϋri, Per, Roos, Sholts, Sabrina B., Rahimipour, Shai, , Karlström, Amelie Eriksson, Gräslund, Astrid, & Wärmländer, Sebastian K. T. S. (2016). Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species. Journal of Alzheimer’s Disease, 54(3), 971–982. https://doi.org/10.3233/jad-160427
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De Geus, D. C., Thomassen, E. A. J., Hagedoorn, P. L., Pannu, N. S., & (2009). 2VXH: The Crystal Structure Of Chlorite Dismutase: A Detox Enzyme Producing Molecular Oxygen. Worldwide Protein Data Bank, 2VXH. https://doi.org/10.2210/pdb2vxh/pdb
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De Geus, D. C., Van Roon, A. M. M., Thomassen, E. A. J., Hokke, C. H., Deelder, A. M., & (2009). 2VQ1: Anti Trimeric Lewis X Fab54-5C10-A. Worldwide Protein Data Bank, 2VQ1. https://doi.org/10.2210/pdb2vq1/pdb
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Pannu, Navraj S., Ravelli, Raimond B. G., & . (2009). The Max-Inf2/Lorentz Center workshop on New algorithms in macromolecular crystallography and electron microscopy. Acta Crystallographica. Section D, Biological Crystallography, 65, 623–624. https://doi.org/10.1107/s0907444909020861
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Waterreus, Willem-Jan, Pannu, Navraj, Skubák, Pavol, Sikharulidze, Irakli, , & de Graaff, R. A. G. (2009). Recent Advances in CRANK [International Union of Crystallography]. Acta Crystallographica A-Foundation and Advances, 65, S160. https://doi.org/10.1107/s0108767309096743
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Jiang, L., & (2008). 3BBU: The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex. Worldwide Protein Data Bank, 3BBU. https://doi.org/10.2210/pdb3bbu/pdb
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Jiang, L., & (2008). 3BBX: The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex. Worldwide Protein Data Bank, 3BBX. https://doi.org/10.2210/pdb3bbx/pdb
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Jiang, L., & (2008). 3BBV: The tRNA(phe) fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex. Worldwide Protein Data Bank, 3BBV. https://doi.org/10.2210/pdb3bbv/pdb
Jiang, L., & (2008). 3BBV: The tRNA(phe) fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex. Worldwide Protein Data Bank, 3BBV. https://doi.org/10.2210/pdb3bbv/pdb
Jiang, Linhua, Schaffitzel, Christiane, Bingel-Erlenmeyer, Rpuven, Ban, Nenad, Korber, Philipp, Koning, Roman I., Plaisier, Jasper R., & . (2008). EMD-1455: Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15. Journal of Molecular Biology, 386(5), 67–1357. https://doi.org/10.1016/j.jmb.2008.10.079
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Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., Plaisier, J. R., & (2008). EMD-1456.map. Electron Microscopy Data Bank, EMD–1456.
Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., Plaisier, J. R., & (2008). EMD-1456.map. Electron Microscopy Data Bank, EMD–1456.
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3C0S: UVDE 3 metals. Worldwide Protein Data Bank, 3C0S. https://doi.org/10.2210/pdb3c0s/pdb
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Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3C0Q: Uvde E175a. Worldwide Protein Data Bank, 3C0Q. https://doi.org/10.2210/pdb3c0q/pdb
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Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3C0L: Uvde K229r. Worldwide Protein Data Bank, 3C0L. https://doi.org/10.2210/pdb3c0l/pdb
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3C0L: Uvde K229r. Worldwide Protein Data Bank, 3C0L. https://doi.org/10.2210/pdb3c0l/pdb
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3BZG: UVDE pH4.4. Worldwide Protein Data Bank, 3BZG. https://doi.org/10.2210/pdb3bzg/pdb
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3BZG: UVDE pH4.4. Worldwide Protein Data Bank, 3BZG. https://doi.org/10.2210/pdb3bzg/pdb
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3BZJ: Uvde K229l. Worldwide Protein Data Bank, 3BZJ. https://doi.org/10.2210/pdb3bzj/pdb
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., , Goosen, N., & Pannu, N. S. (2008). 3BZJ: Uvde K229l. Worldwide Protein Data Bank, 3BZJ. https://doi.org/10.2210/pdb3bzj/pdb
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., , Koerten, H. K., Koning, R. I., & Ban, N. (2008). EMD-1250.map. Electron Microscopy Data Bank, EMD–1250.
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., , Koerten, H. K., Koning, R. I., & Ban, N. (2008). EMD-1250.map. Electron Microscopy Data Bank, EMD–1250.
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., , Koerten, H. K., Koning, R. I., & Ban, N. (2008). EMD-1251: Structure of the E. coli signal recognition particle bound to a translating ribosome. Electron Microscopy Data Bank, EMD–1251.
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., , Koerten, H. K., Koning, R. I., & Ban, N. (2008). EMD-1251: Structure of the E. coli signal recognition particle bound to a translating ribosome. Electron Microscopy Data Bank, EMD–1251.
Zovko, Sandra, , Koster, Abraham J., Galjart, Niels, & Mommaas, A. Mieke. (2008). Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts. Molecular Biology of the Cell, 19(7), 46–3138. https://doi.org/10.1091/mbc.e07-07-0681
Zovko, Sandra, , Koster, Abraham J., Galjart, Niels, & Mommaas, A. Mieke. (2008). Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts. Molecular Biology of the Cell, 19(7), 46–3138. https://doi.org/10.1091/mbc.e07-07-0681
Georgieva, Dilyana G., Kuil, Maxim E., Oosterkamp, Tjerk H., Zandbergen, Henny W., & . (2007). Heterogeneous nucleation of three-dimensional protein nanocrystals. Acta Crystallographica. Section D, Biological Crystallography, 63(Pt 5), 70–564. https://doi.org/10.1107/s0907444907007810
Georgieva, Dilyana G., Kuil, Maxim E., Oosterkamp, Tjerk H., Zandbergen, Henny W., & . (2007). Heterogeneous nucleation of three-dimensional protein nanocrystals. Acta Crystallographica. Section D, Biological Crystallography, 63(Pt 5), 70–564. https://doi.org/10.1107/s0907444907007810
Paspaleva, Keti, Thomassen, Ellen, Pannu, Navraj S., Iwai, Shigenori, Moolenaar, Geri F., Goosen, Nora, & . (2007). Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease. Structure, 15(10), 24–1316. https://doi.org/10.1016/j.str.2007.05.010
Paspaleva, Keti, Thomassen, Ellen, Pannu, Navraj S., Iwai, Shigenori, Moolenaar, Geri F., Goosen, Nora, & . (2007). Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease. Structure, 15(10), 24–1316. https://doi.org/10.1016/j.str.2007.05.010