Joachim Frank

This study identifies the RY12 domain of RyR1 as an ADP sensor and reveals dantrolene's binding mechanism through cryo-EM structures.

The paper determines high-resolution structures of NediV IRES-mediated translation initiation complexes and their transition to elongation, revealing structural changes and interactions during viral translation.

The paper compares ribosome structures of naked mole-rats, tuco-tucos, and guinea pigs, finding fragmented 28S rRNA in the former with potential links to high translational fidelity.

The paper assesses a micro-sprayer assay for ribosome functional activity, finding increased GFP production due to mechanical agitation, with implications for time-resolved cryo-EM experiments.

The paper determines the cryo-EM structure of 48S initiation complexes on EMCV IRESs and identifies key interactions essential for ribosomal recruitment.

The paper identifies inconsistencies in rabbit ribosomal rRNA sequences and proposes using the Broad Institute's genome sequence to standardize numbering and improve model consistency.

This paper introduces a PDMS-based microfluidic chip for time-resolved cryo-EM sample preparation, enabling structural and kinetic studies of biomolecular reactions in the 10-1000 ms time range.

The paper presents cryo-EM structures of Hepatitis C virus IRES initiation complexes, revealing conformational changes during translation initiation.

This study provides structural and functional evidence that NusG links transcription and translation in E. coli by binding both RNA polymerase and the ribosome.

This study uses time-resolved cryo-EM to visualize the conformational changes during bacterial 70S initiation complex formation and maturation into an elongation-competent complex.