We are looking for a post-doc for a collaborative project between the groups of Prof. Leonid Sazanov (IST Austria) and Prof. Michael Wagner/Prof. Holger Daims (University of Vienna) to work on the structures and functions of bioenergetic membrane protein complexes from Nitrospira comammox bacteria. This is a rare chance to uncover “black matter” of several novel large membrane protein complex families with unique properties and unknown structure and mechanism. The recently discovered and environmentally widespread comammox Nitrospira are able to catalyse complete nitrification using a unique respiratory chain. In 2017 the Wagner/Daims groups obtained the only available pure culture of a comammox organism (Nitrospira inopinata) and recently managed to scale up biomass production of these recalcitrant microorganisms to a level that now enables structural characterization of essential protein complexes of these fascinating microbes. 

The Sazanov group is interested in structure and function of large membrane protein complexes from the domain of bioenergetics. We have determined the first structures of respiratory complex I, V/A-type ATPase, transhydrogenase, and MRP antiporters. Prof. Wagner and Prof. Daims are members of the Centre for Microbiology and Environmental Systems Science and their research groups are interested in the biology of nitrifying microorganisms. They have made substantial contributions to better understand the diversity, genomic potential, physiology, and biochemistry of these microbes that play essential roles in the biogeochemical nitrogen cycle of our planet. 

Based on already available biomass, the project will involve purification of complexes (partially established in the lab), followed by cryo-EM structure determination and detailed functional characterisation. The candidate must have a PhD in biochemistry/structural biology with demonstrated (by publications) experience in cryo-EM structure determination. Experience in membrane protein purification or in bioenergetics would be advantageous but is not essential. 

IST Austria is a new multi-disciplinary institute focused on basic research. It has recently been ranked 3rd in the world in research excellence according to Nature Index. Its EM facility includes Krios/K3 and Glacios/FIII TEMs. Infrastructure for protein purification and cryo-EM data processing is state-of-the-art. IST is connected by shuttle bus to Vienna, a top city for quality of life.

The Centre for Microbiology and Environmental Systems Science was founded in 2019 at the University of Vienna and is a research hotspot for microbiology. In total 15 research groups and about 130 scientists from more than 25 countries are active at the Centre. The Centre has unique facilities for the cultivation and functional characterization of microbes including a NanoSIMS and a Raman microfluidics cell sorter. 

The appointment will initially be for 2 years (on a Wittgenstein award grant to Prof. Wagner), with a possibility to extend to 4 years. Starting date is as soon as possible for a suitable candidate. The post holder will be employed in IST Austria, where post-doc salary and benefits are extremely competitive. All queries and applications with CVs and names of 2-3 academic referees should be forwarded to Prof. Leonid Sazanov. Email: [log in to unmask] Homepage: https://ist.ac.at/research/life-sciences/sazanov-group/
Additional queries may be directed to Prof. Wagner at [log in to unmask], Homepage: http://cmess.csb.univie.ac.at/

Recent papers from the Sazanov group on cryo-EM structures and function of bioenergetic membrane proteins:

Kampjut, D. and Sazanov, L.A. (2020) The coupling mechanism of mammalian respiratory complex I. Science, 370(6516):eabc4209. 
Pinke G., Zhou L. and Sazanov L.A. (2020) Cryo-EM structure of the entire mammalian F-type ATP synthase. Nat. Struct. Mol. Biol., 27(11):1077-1085.
Steiner J. and Sazanov L. (2020) Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter. Elife 9, e59407.
Kampjut, D. and Sazanov, L.A. (2019) Structure and mechanism of mitochondrial proton-translocating transhydrogenase. Nature, 573, 291–295.
Zhou, L. and Sazanov, L.A. (2019) Structure and Conformational Plasticity of the Intact Thermus thermophilus V/A-type ATPase. Science, 365, eaaw9144.
Fiedorczuk, K., …, and Sazanov L.A. (2016) Atomic structure of the entire mammalian mitochondrial complex I. Nature, 538, 406-410.
Letts, J.A., Fiedorczuk, K., and Sazanov L.A. (2016) The architecture of respiratory supercomplexes. Nature, 537, 644-648.

Selected papers from the Wagner/Daims groups on comammox microbes and other nitrifiers:

Kits KD, …, Wagner M, Daims H. (2019). Low yield and abiotic origin of N2O formed by the complete nitrifier Nitrospira inopinata. Nat Communications, 1: 1836 

Kits KD, …, Daims H, Wagner M. (2017). Kinetic analysis of a complete nitrifier reveals an oligotrophic lifestyle. Nature, 549: 269-272 

Daims H, …, Wagner M. (2015) Complete nitrification by Nitrospira bacteria. Nature, 528: 504-509 

Palatinszky M, …, Daims H, Wagner M. (2015) Cyanate as an energy source for nitrifiers. Nature, 524: 105-108 

Koch H, …, Wagner M, Daims H. (2014) Growth of nitrite-oxidizing bacteria by aerobic hydrogen oxidation. Science, 345: 1052-1054 

########################################################################

To unsubscribe from the CCPEM list, click the following link:
https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCPEM&A=1

This message was issued to members of www.jiscmail.ac.uk/CCPEM, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/