Skip to main content
Skip banner

Laboratory for Structural Dynamics of Proteins – Dioscuri Centre for Structural Dynamics of Receptors

Dioscuri Center for Structural Dynamics of Receptors was established in 2022 as a result of the 4th edition of the Dioscuri Centers of Scientific Excellence competition financed by the Max Planck Society and the National Science Center Poland.

Dr Przemysław Nogły, associate professor

room: C042 (2.01.31)
phone: +48 12 664 65 91



Dr Theo Battista, Postdoc
room: 1.01.4, phone: +48 12 664 6124, e-mail:

Dr Magdalena Pachota, Postdoc
room: 1.01.4, phone: +48 12 664 6124, e-mail:

Dr Bence Olasz, Postdoc
room: 1.01.4, phone: +48 12 664 6124, e-mail:

Mgr Katarzyna Friedlein-Wójtowicz, Project manager
room: L001, phone: +48 12 664 67 19, mobile: +48 502 015 895, e-mail:

Mgr Aleksandra Solecka, Lab manager 
room: 3.01.06, phone: +48 12 664 67 01, e-mail:

  • Mgr Ayesha Asghar, room: 3.01.06, phone: +48 12 664 67 01, e-mail:

  • Molecular mechanisms of receptors activation
  • Signal transduction
  • Transport mechanism in membrane proteins
  • Development and integration of methods to study protein structural dynamics

  • Crystallography
  • Time-resolved serial crystallography (synchrotrons and X-ray Freel Electron Lasers)
  • Crystallization in Lipidic Cubic Phases
  • Biochemical and biophysical protein characterization
  • Functional assays

  1. Przemyslaw Nogly: Dioscuri Centre for Structural Dynamics of Receptors (2022–2027).  Dioscuri Centres of Scientific Excellence. A programme initiated by the Max Planck Society (MPG), jointly managed with the Polisch National Science Centre (NCN), and mutually funded by the Polich Ministry of Education and Science (MEiN) and the German Federal Ministry of Education and Research (BMBF)

  1. Ultrafast structutral changes direct the first molecular events of vision. Gruhl T, Weinert T, Rodrigues M, Milne CJ, Ortolani G, Nass K, Nango E, Sen S, Johnson PJM, Cirelli C, Furrer A, Mous S, Skopintsev P, James D, Dworkowski F, Båth P, Kekilli D, Ozerov D, Tanaka R, Glover H, Bacellar C, Brünle S, Casadei CM, Diethelm AD, Gashi D, Gotthard G, Guixà-González R, Joti Y, Kabanova V, Knopp G, Lesca E, Ma P, Martiel I, Mühle J, Owada S, Pamula F, Sarabi D, Tejero O, Tsai C, Varma N, Wach A, Boutet S, Tono K, Nogly P, Deupi X, Iwata S, Neutze R, Standfuss J, Schertler G and Panneels V. (2023Nature accepted.
  2. Dynamics and mechanism of a light-driven chloride pump. Mous S, Gotthard G, Ehrenberg D, Sen S, Weinert T, Johnson PJM, James D, Nass K, Furrer A, Kekilli D, Ma P, Brünle S, Casadei CM, Martiel I, Dworkowski F, Gashi D, Skopintsev P, Wranik M, Knopp G, Panepucci E, Panneels V, Cirelli C, Ozerov D, Schertler GFX, Wang M, Milne C, Standfuss J, Schapiro I, Heberle J and Nogly P. (2022Science 375, 845-851
  3. Femtosecond to millisecond structural changes in a light-driven sodium pump. Skopintsev P, Ehrenberg D, Weinert T, James D, Kar R, Johnson P, Ozerov D, Furrer A, Martiel I, Dworkowski F, Nass K, Knopp G, Cirelli C, Arrell C, Gashi D, Mous S, Wranik M, Gruhl T, Kekilli D, Bruenle S, Deupi X, Schertler G, Benoit R, Panneels V, Nogly P, Schapiro I, Milne C, Heberle J and Standfuss J. (2020Nature 583, 314–318
  4. Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Weinert T, Skopintsev P, James D, Dworkowski F, Panepucci E, Kekilli D, Furrer A, Brünle S, Mous S, Ozerov D, Nogly P, Wang M and Standfuss J. (2019Science 365, 61-65
  5. Structural Basis for Allosteric Ligand Recognition in the Human CC Chemokine Receptor 7. Jaeger K, Bruenle S, Weinert T, Guba W, Muehle J, Miyazaki T, Weber M, Furrer A, Haenggi N, Tetaz T, Huang CY, Mattle D, Vonach JM, Gast A, Kuglstatter A, Rudolph MG, Nogly P, Benz J, Dawson RJP and Standfuss J. (2019Cell 178, 1222-1230
  6. Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR. Varma N, Mutt E, Mühle J, Panneels V, Terakita A, Deupi X, Nogly P, Schertler GFX and Lesca E. (2019Proceedings of the National Academy of Sciences 116, 14547-14556
  7. Retinal isomerization in bacteriorhodopsin captured by a femtosecond X-ray laser. Nogly P, Weinert T, James D, Carbajo S, Ozerov D, Furrer A, Gashi D, Borin V, Skopintsev P, Jaeger K, Nass K, Båth P, Bosman R, Koglin J, Seaberg M, Lane T, Kekilli D, Brünle S, Tanaka T, Wu W, Milne C, White T, Barty A, Weierstall U, Panneels V, Nango E, Iwata S, Hunter M, Schapiro I, Schertler G, Neutze R and Standfuss J. (2018) Science 361, 6398
  8. Crystal structure of rhodopsin in complex with a mini-G(o) sheds light on the principles of G protein selectivity. Tsai CJ, Pamula F, Nehmé R, Mühle J, Weinert T, Flock T, Nogly P, Edwards PC, Carpenter B, Gruhl T, Ma P, Deupi X, Standfuss J, Tate CG and Schertler GFX. (2018Science Advances 4, eaat7052
  9. A three-dimensional movie of structural changes in bacteriorhodopsin. Nango E, Royant A, Kubo M, Nakane T, Wickstrand C, Kimura T, Tanaka T, Tono K, Song C, Tanaka R, Arima T, Yamashita A, Kobayashi J, Hosaka T, Mizohata E, Nogly P, Sugahara M, Nam D, Nomura T, Shimamura T, Im D, Fujiwara T, Yamanaka Y, Jeon B, Nishizawa T, Oda K, Fukuda M, Andersson R, Båth P, Dods R, Davidsson J, Matsuoka S, Kawatake S, Murata M,  Nureki O, Owada S, Kameshima T, Hatsui T, Joti T, Schertler G, Yabashi M, Bondar A, Standfuss J, Neutze R and Iwata S. (2016Science 354, 1552-1557
  10. Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography. Nogly P, Panneels V, Nelson G, Gati C, Kimura T, Milne C, Milathianaki D, Kubo M, Wu W, Conrad C, Coe J, Bean R, Zhao Y, Båth P, Dods R, Harimoorthy R, Beyerlein KR, Rheinberger J, James D, DePonte D, Li C, Sala L, Williams G, Hunter M, Koglin JE, Berntsen P, Nango E, Iwata S, Chapman HN, Fromme P, Frank M, Abela R, Boutet S, Barty A, White TA, Weierstall U, Spence J, Neutze R, Schertler G and Standfuss J. (2016Nature Communications 7, 12314