Imperial College London


Faculty of Natural SciencesDepartment of Life Sciences

Chair in Structural Biology



+44 (0)20 7594 3056t.meier Website




501Sir Ernst Chain BuildingSouth Kensington Campus







ATP (adenosine triphosphate) is the universal form of energy in living cells to power biochemical reactions such as muscle contraction or brain function. A human being needs approximately his/her own body weight of ATP per day; this large amount is constantly provided by a rotary ATPase, called the ATP synthase. It functions like an energy converter, which uses electric energy at the cell membrane to convert it in chemical energy, ATP. It is very intriguing that the enzyme works like a mechanic machine that has a rotating ion-turbine and a stator in which the ATP can be generated; The ATP synthase is the smallest "nano-machine" known. We are interested in understanding the structure and operation principles of this remarkable machine and to decipher how it works on the molecular level by using the combined power of sophisticated structural biology methods (X-ray crystallography and electron microscopy).

Rotary ATPase recently came also into focus as new drug target against tuberculosis (TB) and a new antibiotic drug, the first anti-TB drug in the last 40 years, blocks rotation of the ATP synthase's ion turbine. We are therefore also interested in understanding the mechanism of action of these drugs to their target from a biochemical and structural point of view and to develop them further. Our research will also help promoting the molecular understanding and development of drugs against dangerous human infection diseases. For more info, see here:

Research Group

Thomas Meier's Group

Meier lab (August 2017). From right to left:

  • Prof. Dr. Thomas Meier, Group leader
  • Dr. Michael Hohl, Postdoc, SNF Research Fellow
  • Chi Wong, Research Technician
  • Lisa Uhrig, PhD student
  • Dr. Julius Demmer, Postdoc
  • Dr. Yilmaz Alguel, Postdoc



Eisel B, Hartrampf FWW, Meier T, et al., 2018, Reversible optical control of F1 Fo -ATP synthase using photoswitchable inhibitors., Febs Lett, Vol:592, Pages:343-355

Schulz S, Wilkes M, Mills DJ, et al., 2017, Molecular architecture of the N-type ATPase rotor ring from Burkholderia pseudomallei, Embo Reports, Vol:18, ISSN:1469-221X, Pages:526-535

He C, Preiss L, Wang B, et al., 2017, Structural Simplification of Bedaquiline: the Discovery of 3-(4-(N,N-Dimethylaminomethyl)phenyl)quinoline-Derived Antitubercular Lead Compounds, Chemmedchem, Vol:12, ISSN:1860-7179, Pages:106-119

Hahn A, Parey K, Bublitz M, et al., 2016, Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology, Molecular Cell, Vol:63, ISSN:1097-2765, Pages:445-456

Preiss L, Hicks DB, Suzuki S, et al., 2015, Alkaliphilic Bacteria with Impact on Industrial Applications, Concepts of Early Life Forms, and Bioenergetics of ATP Synthesis, Frontiers in Bioengineering and Biotechnology, Vol:3

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