Ieva Drulyte
@ievadr.bsky.social
1.2K followers
350 following
340 posts
Structural biologist | CryoCloud 🔬☁️ | Posts about #cryoEM, some running and cats | Views my own | She/her
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Reposted by Ieva Drulyte
Yikes! In this paper the AlphaFold model of human plasminogen (PDB-8uq6) has been refined into noise (EMD-42462) using Phenix & ISOLDE. For some reason the authors even interpret side-chain interactions:
#cryoEM
#cryoEM
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Ieva Drulyte
@ievadr.bsky.social
· Sep 19
Thrilled to welcome Dr Joshua White as Senior Application Scientist at CryoCloud! With deep expertise in single-particle analysis & end-to-end #cryoEM workflows, Josh will lead data analysis, user training & support. Excited to have his experience & energy on board! 🚀
@jbrwhite.bsky.social
@jbrwhite.bsky.social
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Sjors Scheres
@sjorsscheres.bsky.social
· Aug 12
Cryo-EM structure of the vault from human brain reveals symmetry mismatch at its caps
Lövestam and Scheres present a cryo-EM structure of vault particles, found during
tau filament extraction from progressive supranuclear palsy (PSP) brain tissue. They
reveal a symmetry shift at the va...
www.cell.com
Reposted by Ieva Drulyte
SCIENMAG
@scienmag.bsky.social
· Aug 8
Cryo-EM Structures Uncover Diverse L and P Protein Interactions in Nipah Virus Polymerase Among Paramyxoviruses
In a groundbreaking advance that significantly deepens our understanding of viral replication machinery, researchers have unveiled high-resolution cryo-electron microscopy (cryo-EM) structures of the Nipah virus (NiV) polymerase complex. This detailed structural insight opens new avenues for the design of antiviral agents targeting a highly pathogenic zoonotic virus responsible for severe and often fatal human infections. Nipah virus, an emergent member of the Paramyxoviridae family, poses a persistent public health threat due to its zoonotic nature and the absence of approved therapeutics.
scienmag.com
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Shicheng Guo
@shihcheng.bsky.social
· Aug 3
Cryo-EM structure of native honey bee vitellogenin | Nature Communications
Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalitie
doi.org
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Reposted by Ieva Drulyte
Basil Greber
@bjgreber.bsky.social
· Jul 30
Sub-3 Å resolution protein structure determination by single-particle cryo-EM at 100 keV
Cryoelectron microscopy (cryo-EM) has transformed structural biology by providing high-resolution insights into biological macromolecules. We report s…
www.sciencedirect.com