Adriana Klyszejko

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Industrial Liaison Scientist - Cryo-Electron Microscopy

Email: industry@diamond.ac.uk
Tel: +44 (0)1235 778995

Cryo-Electron Microscopy

 

Latest Publications

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  1. Biography
  2. Scientific Interests
  3. Publications
Biography -

Biography

Adriana joined the Industrial Liaison Office in November 2019 as a cryo Electron Microscopy scientist to support industry clients throughout sample preparation, data acquisition and structure determination using latest generation microscopes at electron Bio-Imaging Centre for Industry, eBIC4i.
She has experience in both classic and advanced blot-free sample preparation techniques for electron microscopy. Before joining our team, Adriana worked on method development for cryo EM as a postdoc at eBIC. She joined Diamond in May 2018 from the Astbury Centre for Structural Molecular Biology at the University of Leeds, where she studied muscle proteins by negative staining and cryo EM.
Previously, Adriana worked as a postdoc in the Max Planck Institute of Biophysics in Frankfurt am Main, Germany, where she studied assembly of the F-type ATP synthase using Atomic Force Microscopy. She obtained her PhD at the Technische Universität Dresden, Germany, where she studied structure and assembly of various membrane proteins by AFM at the Biotechnology Center (BIOTEC).
In 2013–2016, Adriana was an invited member of the Scanning Probe Microscopy Section of the Royal Microscopical Society.
On top of her strong background in structural biology, Adriana strengthens our team with her extensive experience in cutting-edge sample preparation techniques, including practical knowledge of expression systems and protein purification from native mammalian tissues combined with her background in microbiology.

  

Scientific Interests - +

Scientific Interests

cryo-electron microscopy, sample preparation and single particle cryo-EM.

Publications - +

Publications

Matthies D, Zhou W, Klyszejko AL et al. High-resolution structure and mechanism of a F/V hybrid rotor ring in a Na⁺-coupled ATP synthase. Nat Commun. 2014;5:5286.
 
Preiss L, Klyszejko AL et al. The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4. Proc.Nat.Acad.Sci.USA 2013;110(19):7874-9.
 
Hakulinen JK, Klyszejko AL et al. Structural study on the architecture of the bacterial ATP synthase Fo motor. Proc.Nat.Acad.Sci.USA 2012;109(30):E2050-6.
 
Pogoryelov D, Klyszejko AL et al. Engineering rotor ring stoichiometries in the ATP synthase. Proc.Nat.Acad.Sci.USA 2012;109(25):E1599-608.
 
Matthies D, Preiss L, Klyszejko AL, et al. The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region.J.Mol.Biol. 2009;388(3):611-8.
 
Klyszejko AL, Shastri S et al. Folding and assembly of proteorhodopsin. J.Mol.Biol. 2008;376(1):35-41.
 
Fritz M, Klyszejko AL et al. An intermediate step in the evolution of ATPases: a hybrid F0-V0 rotor in a bacterial Na+ F1F0 ATP synthase. FEBS J. 2008;275(9):1999-2007.
 
Pogoryelov D, Reichen C, Klyszejko AL et al. The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15. J.Bacteriol. 2007;189(16):5895-902.
 
Klyszejko A et al. Mycological analysis of cereal samples and screening of Fusarium strains' ability to form deoxynivalenole (DON) and zearalenone (ZEA) mycotoxins-a pilot study. Pol.J.Microbiol. 2005;54 Suppl:21-5.
 
PUBLISHED CONFERENCE ABSTRACTS
 
Pogoryelov D, Klyszejko AL et al. Engineering rotor ring stoichiometries in the ATP synthase. Biochim.Biophys.Acta-Bioenergetics 2012;1817:S21-S21.
 
Matthies D, Klyszejko, AL et al. Structure of the Fo/Vo-hybrid ATP synthase rotor ring from Acetobacterium woodii at 2.4 angstrom resolution. Biochim.Biophys.Acta-Bioenergetics 2012;1817:S19-S19.
 
Matthies D, Preiss L, Morgner N, Klyszejko, AL et al. Structural studies of the membraneembedded c-ring of the FIFO-ATP synthase from a thermoalkaliphilic bacterium reveal a strategy for adaptation to alkaline environments. Biochim.Biophys.Acta-Bioenergetics 2010;1797:S36S-36. 

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