Dear colleagues, I would be grateful if you could bring the following ad for a post-doctoral position in my lab to the attention of suitable candidates.
Kind regards, Inari Kursula *** Post-doctoral position in the group of Inari Kursula at the Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland We have an opening for an enthusiastic post-doctoral fellow to study the molecular mechanisms governing actin polymerization, ATP hydrolysis, phosphate release, and filament stability in malaria parasite actins. The successful candidate has a keen interest to understand cytoskeletal proteins and cell motility in depth. A strong background in protein biochemistry and X-ray crystallography is required. Expertise in cryo-EM sample preparation and structure determination will be highly valued. In addition, a high level of own initiative and the ability to work in a team and supervise younger scientists are necessary. The Faculty of Biochemistry and Molecular Medicine (FBMM; https://www.oulu.fi/fbmm/) is a dynamic and international working place, where the working language is English. Protein science is one of the focal areas of the Faculty. FBMM provides cutting-edge research facilities for molecular biology, protein biochemistry, X-ray crystallography, and light and electron microscopy. In addition, we have generous access to several large-scale facilities for structural biology (MX/SAXS/cryo-EM). Funding is initially available for 2.5 years, but there may be possibilities for an extension. The starting date should be as soon as possible. Applications and informal enquiries should be sent by e-mail to inari.kurs...@oulu.fi. Applications should contain (i) a cover letter detailing your specific interest in this project and your key skills and expertise, (ii) a CV including a list of publications, and (iii) contact information (e-mail) for 3 referees. Applications should preferably be sent by 30.4.2019, but screening of candidates will continue until a suitable one has been identified. For more information on our work, please visit our website: http://cc.oulu.fi/~inkursul/lab Some recent publications directly relevant for the topic: Kumpula EP, Lopez AJ, Tajedin L, Han H & Kursula I (2018) Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and phosphate release. bioRxiv: 467423, https://doi.org/10.1101/467423. Kumpula EP, Pires IP, Lasiwa D, Piirainen H, Bergmann U, Vahokoski J & Kursula I (2017) Apicomplexan actin polymerization depends on nucleation. Sci Rep 7: 12137. Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I & Raunser S (2017) Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proc Natl Acad Sci 114: 10636-10641. Green JL, Wall RJ, Vahokoski J, Yusuf NA, Ridzuan MAM, Stanway RR, Stock J, Knuepfer E, Brady D, Martin SR, Howell SA, Pires IP, Moon RW, Molloy JE, Kursula I, Tewari R & Holder AA (2017) Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility. J Biol Chem 292: 17857-17875. For a full list of publications from our group, see: http://cc.oulu.fi/~inkursul/lab/Molecular_mechanisms_of_actin-based_motility/publications.html *** -------------------------------------------------------------------------------------- Prof. Inari Kursula Department of Biomedicine University of Bergen Jonas Lies vei 91 5009 Bergen Norway Faculty of Biochemistry and Molecular Medicine University of Oulu Aapistie 7 90220 Oulu Finland European XFEL GmbH Holzkoppel 4 22869 Schenefeld Germany http://cc.oulu.fi/~inkursul/lab inari.kurs...@uib.no, inari.kurs...@oulu.fi, inari.kurs...@xfel.eu Tel. +47 5558 6846, +49 40 8998 6862 -------------------------------------------------------------------------------------- ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
