Researcher Portfolio

 
   

Buschmann, Sabine

Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society  

 

Researcher Profile

 
Position: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society
Additional IDs: ORCID: https://orcid.org/0000-0003-0430-4477
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons137616

External references

 
WorldCat Search for Buschmann, Sabine
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Publications

 
 
 : Kalavacherla, T., Buschmann, S., Schleker, E. S. M., Michel, H., & Reinhart, C. (2023). Purification and characterization of eukaryotic ATP-dependent transporters homologously expressed in Pichia pastoris for structural studies by cryo-electron microscopy. Protein Expression and Purification, 204: 106230. doi:10.1016/j.pep.2023.106230. [PubMan] : Schleker, E. S. M., Buschmann, S., Xie, H., Welsch, S., Michel, H., & Reinhart, C. (2022). Structural and functional investigation of ABC transporter STE6-2p from Pichia pastoris reveals unexpected interaction with sterol molecules. Proceedings of the National Academy of Sciences of the United States of America, 126(43), 8646-8654. doi:10.1073/pnas.2202822119. [PubMan] : Xie, H., Muenke, C., Sommer, M., Buschmann, S., & Michel, H. (2022). Production of Membrane Proteins in Pseudomonas stutzeri. In I. Mus-Veteau (Ed.), Methods in Molecular Biology (pp. 91-110). New York, NY: Humana Press. doi:10.1007/978-1-0716-2368-8_6. [PubMan] : Grund, T. N., Radloff, M., Wu, D., Goojani, H. G., Witte, L. F., Jösting, W., Buschmann, S., Müller, H., Elamri, I., Welsch, S., Schwalbe, H., Michel, H., Bald, D., & Safarian, S. (2021). Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 118(50): e2114013118. doi:10.1073/pnas.2114013118. [PubMan] : Kohlstädt, M., Buschmann, S., Langer, J. D., Xie, H., & Michel, H. (2017). Subunit CcoQ is involved in the assembly of the Cbb3-type cytochrome c oxidases from Pseudomonas stutzeri ZoBell but not required for their activity. Biochimica et Biophysica Acta, Bioenergetics, 1858(3), 231-238. doi:10.1016/j.bbabio.2016.12.006. [PubMan] : Kohlstädt, M., Buschmann, S., Xie, H., Resemann, A., Warkentin, E., Langer, J. D., & Michel, H. (2016). Identification and characterization of the novel subunit CcoM in the cbb3-cytochrome c oxidase from Pseudomonas stutzeri ZoBell. mBio, 7(7), 1-9. doi:10.1128/mBio.01921-15. [PubMan] : Buschmann, S., Richers, S., Ermler, U., & Michel, H. (2014). A decade of crystallization drops: Crystallization of the cbb3 cytochrome c oxidase from Pseudomonas stutzeri. Protein Science, 23(4), 411-422. doi:10.1002/pro.2423. [PubMan] : Xie, H., Buschmann, S., Langer, J. D., Ludwig, B., & Michel, H. (2014). Biochemical and Biophysical Characterization of the Two Isoforms of cbb3-Type Cytochrome c Oxidase from Pseudomonas stutzeri. Journal of Bacteriology (Washington, DC), 196(2), 472-482. doi:10.1128/JB.01072-13. [PubMan] : Buschmann, S., Warkentin, E., Xie, H., Langer, J. D., Ermler, U., & Michel, H. (2010). The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping. Science, 329(5989), 327-330. doi:10.1126/science.1187303. [PubMan]