Major Research Interests
The work in our group is focused on 3D structure determination of large macromolecular complexes by single particle electron cryomicroscopy (cryo-EM). In cryo-EM, thousands of electron microscopical images of a macromolecular complex are taken at low temperature in the electron microscope and are used to calculate a 3D reconstruction of the object by computational image processing. Electron microscopical images can be considered as almost ideal two-dimensional projection images, similar to images obtained by computer tomography in medical applications. However, in cryo-EM the relative orientation of the molecules is a priori unknown and must be determined by computational meansprior to calculating the 3D structure. Cryo-EM is the method of choice for 3D structure determination of macromolecular complexes that are difficult to purify in the amounts and quality that is required for crystallization (X-ray crystallography). Due to the low copy number of many functionally important macromolecular complexes in the cell, cryo- EM is very often the only available method to study the 3D structure of these large macromolecules. Work in our group concentrates on macromolecular complexes related to pre-mRNA splicing, translation and cell cycle regulation and on the development of new methods to improve sample preparation, imaging and computational image processing techniques.






Homepage Department/Research Group
http://www.mpibpc.mpg.de/groups/stark/

Selected Recent Publications

• Fischer N, Konevega AL, Wintermeyer W, Rodnina MV, Stark H (2010) Ribosome dynamics and tRNA movement as visualized by time-resolved electron cryomicroscopy. Nature 466, 329-333


• Schmeisser M, Heisen BC, Luettich M, Busche B, Hauer F, Koske T, Knauber KH, Stark H (2009) Parallel, distributed and GPU computing technologies in single-particle electron microscopy. Acta Crystallogr D Biol Crystallogr 65(Pt 7): 659-71


• Wolf E, Kastner B, Deckert J, Merz C, Stark H, Luhrmann R (2009) Exon, intron and splice site locations in the spliceosomal B complex. EMBO J 28(15): 2283- 2292


• Lührmann R, Stark H (2009) Structural mapping of spliceosomes by electron microscopy. Curr Opin Struct Biol 19(1): 96-102


• Chari A, Golas MM, Klingenhager M, Neuenkirchen N, Sander B, Englbrecht C, Sickmann A, Stark H, Fischer U (2008) An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell 135(3): 497- 509