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....
Congratulations Dr. Ming Sun
Congratulations to Dr. Ming Sun for her successful...

New paper accepted by Cell
Structural basis for gating and activation of RyR1. by...

New paper in Science
Elucidation of AMPA receptor–stargazin complexes...