For decades, how methanogenic archaea activate the MCR complex to produce methane remained a mystery. Today in Nature, we report the high-resolution cryo-EM structure of the MCR activation complex! 🥳🥳 https://t.co/XoRagF4Trb

New preprint - basically we noticed that by applying ab initio (SDG) at high res in CS, using a very small step size, we could crack some small proteins we hadn't been able to solve before. Read the preprint or head over to bluesky for a longer thread! https://t.co/aTe4bNxmuf

It is out now 🥳🥂 I am very happy to be part of this nice collaboration in which we were able to characterize different bacterial chemoreceptors and their ligand specificities. Amazing teamwork with Wenhao Xu, @sourjik, @BangeBalcony, et. al 🤩 👇👇👇 https://t.co/JNRVTOO0DR

I am honored and excited that our research on #nitrogenases and the conversion of #CO2 to hydrocarbons is highlighted in the Yearbook 2024 of the Max Planck Society, see page 29. An English and a German version of the Yearbook are available https://t.co/n6MX63Ndm5.

New paper from the lab from @SriramGarg. We introduce a general substitution matrix for structural phylogenetics. I think this is a big deal, so read on below if you think deep history is important.

How do cells "decide" their fate from growth factor signals? Our new study introduces signaling homeorhesis — a dynamic alternative to homeostasis — to explain how cells interpret pulsatile signals into phenotypes. #CellBiology #CellSignaling

Nature research paper: Structure of the ATP-driven methyl-coenzyme M reductase activation complex https://t.co/scvaOyePPt

I'm truly excited to announce our new publication in @Nature unraveling a central picture of the Methyl-coenzyme M reductase (MCR) activation machinery and it's strong ATP dependency - kudos to @AnujR2d2 for the fantastic illustration! LINK: https://t.co/OmMRWWtNR8

This is a wild paper. The anaerobic biochemistry is definitely worth your while (and beyond me to explain), but let me try to explain why this is also an evolutionary bombshell. This is about how nitrogen fixation evolved as we know it.

Check out this fantastic thread from @fidelormz about out latest work out in Nature!! 🥳🥳

@fidelormz @sophia_pa_ I thank @SchullerJm for leading the team and conceptualising the project, and special thanks to @stripplab.bsky.social, Silvan, and @KaHochberg Also many thanks to Stefan for giving us generous access to kriosG4!!

This was a great effort and collaboration between me and my fellow co–first authors, @fidelormz and @sophia_pa_ 🥳🥳🥳 A blender image nicely illustrates our work :)

Take a moment to check the most recent publication by @AnujR2d2 et al., about the structure & mechanism of a major respiratory complex in anaerobes 👇🏼

Excited to share our latest work on the structure and mechanism of the ancient sodium-pumping Rnf complex, now out in @NatureComms

Very proud to share our latest work on the ancient the Na+-pumping Rnf complex – now out in Nature Comms. Thank you Schuller & Müller Labs for great collaboration, and @KAWstiftelsen for generous funding https://t.co/0zCeWXUbuT

Two exciting papers about the the protection of nitrogenases from O2 by the ferredoxin Shethna protein II from the Tezcan https://t.co/eTrdlbNFDx and Einsle https://t.co/8AG7FmKCHM labs were published today by @Nature. Surprisingly both papers reveal superstructures of filaments.

Great work from my colleague @TomasPascoa

Our latest work on a #nitrogenase-like enzyme, the methylthio-alkane reductase which surprisingly also contains large nitrogenase metalloclusters, the P-cluster and the [Fe8S9C]- (L)-cluster is now online: https://t.co/k6E8Sf1A99 Have a look at the 🧵 by @AnaLagoMaciel.

I will be hiring officially later this year, but if you are interested in pursuing a Phd focused on metalloenzymes and infrared spectroscopy... Give me call!

Moreover, we will explore the role of [FeFe]-hydrogenase in multienzyme complexes, e.g., driving CO2 and CO reduction via H2 oxidation and electron bifurcation.