Tristan Reif-Trauttmansdorff

The paper investigates the structure and dynamics of the archaeal ACDS complex, revealing a mechanism for efficient carbon transfer through transient interactions rather than stable complexes.

The paper presents cryo-EM structures of the Mtr complex from Methanosarcina mazei, revealing a novel [Fe8S9C] cluster near the catalytic site and suggesting a link between methyl transfer and Na+ translocation.

This study reveals how BCRII enzymes use electron-bifurcation modules to reduce aromatic rings beyond typical biological redox limits.

This study presents the first molecular structure of methylthio-alkane reductase, revealing metalloclusters that inform its function and evolutionary relationship to nitrogenases.

The paper presents a cryo-EM structure of the Mtr complex from Methanosarcina mazei and identifies a small ORF protein, MtrI, involved in oxygen stress response.

This study shows that 2-oxoglutarate induces dodecamer assembly of Methanosarcina mazei glutamine synthetase, enhancing its activity through a cooperative mechanism.

This study elucidates the molecular mechanism of redox-coupled sodium pumping in the Rnf complex using cryo-EM, biochemical assays, and simulations.

This paper develops exonuclease-deficient cell-free extracts and optimized buffers to enable robust expression from unprotected linear DNA without additional protection strategies.