Discover and read the best of Twitter Threads about #RELION
Most recents (3)
As this thread is gathering all kinds of perspectives, below are mine, including on a bit of history. But before that, just to say that I very much value the hard work by all the people who make #cryoEM image processing better for everyone, both in academia and in industry.
In 2012, I introduced a regularised likelihood approach for #cryoEM structure determination, which formed the basis for #RELION. This approach proved to be hugely successful and is now the basis of many software packages, including also #cryoSPARC.
sciencedirect.com/science/articl…
sciencedirect.com/science/articl…
When #RELION started to replace #EMAN and #SPIDER, and before #cryoSPARC, I expressed in multiple talks that the #cryoEM field needed more diversity in software, as a monoculture is vulnerable. I used the picture below in my talk at the 2014 NRAMM course.
Very proud that our manuscript on the assembly and aging of actin filaments (and my first publication as a postdoc) is finally online @Nature (open access!)
nature.com/articles/s4158…
This was a great team effort from the @Intein lab @mpimoph.
A thread (1/17)
nature.com/articles/s4158…
This was a great team effort from the @Intein lab @mpimoph.
A thread (1/17)
Actin is a highly abundant protein and a major component of the eukaryotic cytoskeleton. It exists in two main forms, as monomer (G-actin) and as filament (F-actin). The dynamic turnover of actin filaments is crucial for controlling cell shape, polarity and movement.
(2/17)
(2/17)
After polymerization, F-actin rapidly hydrolyzes ATP and undergoes transitions dependent on its bound nucleotide. 'Aged' ADP-F-actin can be depolymerized back to G-actin.
We aimed to visualize and understand F-actin assembly and aging at the highest molecular detail.
(3/17)
We aimed to visualize and understand F-actin assembly and aging at the highest molecular detail.
(3/17)
New preprint from the lab: "High-resolution cryo-EM using beam-image shift at 200 keV." Take home message: even with a pretty poorly aligned #cryoEM instrument, you can overcome these aberrations computationally with #RELION (1/n) biorxiv.org/content/10.110…
This came from me asking many people: what is the limit for using beam-image shift to collect data at 200 keV? Everyone said it should be worse at 200 keV than 300 keV but we were surprised no one had benchmarked this yet
So! @annotated_sci set to it - collecting an aldolase dataset on our Talos-Arctica. A part of this work was that we did not do any microscope alignments day-of, simulating what a 'worse case' scenario could be for the instrument.
