Fort, Kyle L., van de Waterbeemd, Michiel, Boll, Dmitriy, Reinhardt-Szyba, Maria, Belov, Mikhail E., Sasaki, Eita, Zschoche, Reinhard, Hilvert, Donald, Makarov, Alexander A., Heck, Albert J. R. (2018) Expanding the structural analysis capabilities on an Orbitrap-based mass spectrometer for large macromolecular complexes. The Analyst, 143 (1). 100-105 doi:10.1039/c7an01629h

See Also

These are possibly similar items as determined by title/reference text matching only.

	van de Waterbeemd, Michiel, Fort, Kyle L, Boll, Dmitriy, Reinhardt-Szyba, Maria, Routh, Andrew, Makarov, Alexander, Heck, Albert J R (2017) High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles. Nature Methods, 14 (3). 283-286 doi:10.1038/nmeth.4147
	Sasaki, Eita, Böhringer, Daniel, van de Waterbeemd, Michiel, Leibundgut, Marc, Zschoche, Reinhard, Heck, Albert J. R., Ban, Nenad, Hilvert, Donald (2017) Structure and assembly of scalable porous protein cages. Nature Communications, 8. doi:10.1038/ncomms14663
	van de Waterbeemd, Michiel, Tamara, Sem, Fort, Kyle L., Damoc, Eugen, Franc, Vojtech, Bieri, Philipp, Itten, Martin, Makarov, Alexander, Ban, Nenad, Heck, Albert J. R. (2018) Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods. Nature Communications, 9. doi:10.1038/s41467-018-04853-x
	Mathew, Anjusha, Giskes, Frans, Lekkas, Alexandros, Greisch, Jean-François, Eijkel, Gert B., Anthony, Ian G. M., Fort, Kyle, Heck, Albert J. R., Papanastasiou, Dimitris, Makarov, Alexander A., Ellis, Shane R., Heeren, Ron M. A. (2023) An Orbitrap/Time-of-Flight Mass Spectrometer for Photofragment Ion Imaging and High-Resolution Mass Analysis of Native Macromolecular Assemblies. Journal of the American Society for Mass Spectrometry, 34 (7) 1359-1371 doi:10.1021/jasms.3c00053
	Snijder, Joost, van de Waterbeemd, Michiel, Damoc, Eugen, Denisov, Eduard, Grinfeld, Dmitry, Bennett, Antonette, Agbandje-McKenna, Mavis, Makarov, Alexander, Heck, Albert J. R. (2014) Defining the Stoichiometry and Cargo Load of Viral and Bacterial Nanoparticles by Orbitrap Mass Spectrometry. Journal Of The American Chemical Society, 136 (20) 7295-7299 doi:10.1021/ja502616y
	Wörner, Tobias P., Aizikov, Konstantin, Snijder, Joost, Fort, Kyle L., Makarov, Alexander A., Heck, Albert J. R. (2022) Frequency chasing of individual megadalton ions in an Orbitrap analyser improves precision of analysis in single-molecule mass spectrometry. Nature Chemistry, 14 (5) 515-522 doi:10.1038/s41557-022-00897-1
	Neumann, Adam P., Sage, Eric, Boll, Dmitri, Reinhardt‐Szyba, Maria, Fon, Warren, Masselon, Christophe, Hentz, Sébastien, Sader, John E., Makarov, Alexander, Roukes, Michael L. (2024) A Hybrid Orbitrap‐Nanoelectromechanical Systems Approach for the Analysis of Individual, Intact Proteins in Real Time. Angewandte Chemie, 136 (33) doi:10.1002/ange.202317064
	Neumann, Adam P., Sage, Eric, Boll, Dmitri, Reinhardt‐Szyba, Maria, Fon, Warren, Masselon, Christophe, Hentz, Sébastien, Sader, John E., Makarov, Alexander, Roukes, Michael L. (2024) A Hybrid Orbitrap‐Nanoelectromechanical Systems Approach for the Analysis of Individual, Intact Proteins in Real Time. Angewandte Chemie International Edition, 63 (33) doi:10.1002/anie.202317064
	VanAernum, Zachary L., Gilbert, Joshua D., Belov, Mikhail E., Makarov, Alexander A., Horning, Stevan R., Wysocki, Vicki H. (2019) Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer. Analytical Chemistry, 91 (5). 3611-3618 doi:10.1021/acs.analchem.8b05605
	Peris-Díaz, Manuel D.; Barendregt, Arjan; Wörner, Tobias P.; Fort, Kyle L.; Makarov, Alexander A.; Deslignière, Evolène; Heck, Albert J. R. (2025) Electron Capture-Induced Charge Reduction Benefits the Recording of Ultralong Transients in Orbitrap-Based Individual-Ion Mass Spectrometry. Analytical Chemistry, 97 (22). doi:10.1021/acs.analchem.5c01000
	Rose, Rebecca J, Damoc, Eugen, Denisov, Eduard, Makarov, Alexander, Heck, Albert J R (2012) High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies. Nature Methods, 9 (11). 1084-1086 doi:10.1038/nmeth.2208