Welcome to Frank Lab
We investigate the mechanism of translation on the ribosome by using cryo-electron microscopy and single-particle reconstruction.
Recent Publications
Article: Structural Basis for Gating and Activation of RyR1
Journal: Cell
Authors: Amédée des Georges, et al.
[Abstract]
Article: Elucidation of AMPA receptor–stargazin complexes by
cryo–electron microscopy
Journal: Science
Authors: Edward C. Twomey, et al.
[Abstract]
Article: Whither Ribosome Structure and Dynamics Research?
(A Perspective)
Journal: Journal of Molecular Biology
Authors: Joachim Frank
[Abstract]
Article: Continuous Changes in Structure Mapped by Manifold Embedding
of Single-Particle Data in Cryo-EM
Journal: Methods
Authors: Joachim Frank, Abbas Ourmazd
[Abstract]
Article: Generalized single-particle cryo-EM – a historical perspective
Journal: Microscopy
Authors: Joachim Frank
[Abstract]
Article: Dynamical features of the Plasmodium falciparum ribosome
during translation
Journal: Nucleic Acids Research Journal
Authors: Ming Sun, et al.
[Abstract]
Article: Structure of mammalian eIF3 in the context of the 43S
preinitiation complex
Journal: Nature
Authors: Amedee Des Georges, et al.
[Abstract]
Article: Structural dynamics of ribosome subunit association studied by
mixing-spraying time-resolved cryo-EM
Journal: Structure
Authors: Bo Chen, et al.
[Abstract]
Article: Activation of GTP Hydrolysis in mRNA-tRNA Translocation by
Elongation Factor G
Journal: Science Advances
Authors: Wen Li, et al.
[Abstract]
Article: Efficient estimation of three-dimensional covariance and its application
in the analysis of heterogeneous samples in cryo-electron microscopy
Journal: Structure
Authors: Hstau Y. Liao, et al.
[Abstract]
Recent News
Structural Basis for Gating and Activation of RyR1
September 23, 2016
Our long-awaited Cell article on the activation and gating mechanism of the skeletal Ryanodine receptor RyR1 (a.k.a. calcium release channel) has finally appeared in Cell [1]. It is based on the highest-resolution maps obtained so far (up to 3.6 Å), which depict the channel in several states induced by the binding of calcium, ATP and caffeine, including a fully open state. The atomic structures determined from these density maps allowed us to infer the mechanisms of channel activation and gating, as sketched out in the graphical abstract below....
