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Dear CCP4BB-Users, On behalf of Prof. Thilo Stehle I would like to post a job offer for two PhD positions at the Interfaculty Institute of Biochemistry. Best Regards, Georg
##### PhD
positions in Structural Biology at the Interfaculty
Institute of
Biochemistry The successful candidates will work on the structural and functional characterization of virus-glycan interactions and on the structural and functional analysis of enzymes involved in cell wall synthesis and degradation in pathogenic bacteria (see selected publications below for examples of our work). We seek highly motivated individuals with a Master degree in a relevant field (e.g. biochemistry or chemistry). The ideal candidates will have practical and theoretical knowledge in construct design and optimization as well as protein production and purification. Experience in structure determination methods and other biophysical methods is an advantage. We expect excellent communication skills, willingness to work in a team, dedication and motivation and the ability to design, plan and interpret experiments in an independent manner. The ability to communicate in english is essential, and a good working knowledge of german will be advantageous but is not mandatory. The salary will be based on German federal TV-L 13 (65%). The positions are fully funded and available immediately. Applications will be considered until July 15, 2019. The University of Tübingen is an equal-opportunity employer and is committed to employ more handicapped individuals and especially encourages them to apply. Applications of women are explicitly encouraged. Applications including contact information (E-mail, phone, or Skype), CV, research experience, copy of the Master degree certificate, and contact information of two persons for references should be send as single pdf document (max. size 3 MB) to apply2stehle@gmail.com
References: Gerlach et al. (2018). Methicillin-resistant Staphylococcus aureus alters cell wall glycosylation to evade immunity. Nature 563, 705-709. Lenman et al. (2018). Polysialic acid is a cellular receptor for human adenovirus 52. Proc. Natl. Acad. Sci. U S A. 115, E4264-E4273 Ströh et al. (2015). Trichodysplasia Spinulosa-associated Polyomavirus Uses a Displaced Binding Site on VP1 to Engage Sialylated Glycolipids. PLoS Pathog. 11, e1005112. Blaum et al. (2015). Structural basis for sialic acid-mediated self-recognition by complement factor H. Nat. Chem. Biol. 11, 77-82.
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