WikiSysop: Created page with "== Citation == Wang, T., Li, Z., Xu, K., Huang, W., Huang, G., Zhang, Q.C. and Yan, N. 2024. CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy. Proceedings of the National Academy of Sciences. 121, 42 (2024), e2417046121. == Abstract == Structural biology is experiencing a paradigm shift from targeted structural determination to structure-guided discovery of previously uncharacterized bioentities. We employed cryoelectron microscopy (cryo-EM)..."

2026-07-22T06:46:51Z

Created page with "== Citation == Wang, T., Li, Z., Xu, K., Huang, W., Huang, G., Zhang, Q.C. and Yan, N. 2024. CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy. Proceedings of the National Academy of Sciences. 121, 42 (2024), e2417046121. == Abstract == Structural biology is experiencing a paradigm shift from targeted structural determination to structure-guided discovery of previously uncharacterized bioentities. We employed cryoelectron microscopy (cryo-EM)..."

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== Citation ==

Wang, T., Li, Z., Xu, K., Huang, W., Huang, G., Zhang, Q.C. and Yan, N. 2024. CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy. Proceedings of the National Academy of Sciences. 121, 42 (2024), e2417046121.

== Abstract ==

Structural biology is experiencing a paradigm shift from targeted structural determination
to structure-guided
discovery of previously uncharacterized bioentities. We
employed cryoelectron microscopy (cryo-EM)
to analyze filtered water samples collected
from the Tsinghua Lotus Pond. Here, we report the structural determination and
characterization of two highly similar helical fibrils, named TLP-1a
and TLP-1b,
each
approximately 8 nm in diameter with a 15-Å
wide tunnel. These fibrils are assembled
from a similar protein protomer, whose structure was conveniently automodeled in
CryoNet. The protomer structure does not match any available experimental structures,
but shares the same fold as many predicted structures of unknown functions.
The amino-terminal
β strand of protomer n + 4 inserts into a cleft in protomer n to
complete an immunoglobulin (Ig)-like
domain. This packing mechanism, known as
donor-strand
exchange (DSE), has been observed in several bacterial pilus assemblies,
wherein the donor is protomer n + 1. Despite distinct shape and thickness, this reminiscence
suggests that TLP-1a/
b fibrils may represent uncharacterized bacterial pili. Our
study demonstrates an emerging paradigm in structural biology, where high-resolution
structural determination precedes and drives the identification and characterization of
completely unknown objects.

== Keywords ==

== Links ==

https://www.pnas.org/doi/abs/10.1073/pnas.2417046121

== Related software ==

== Related methods ==

== Comments ==

2024Wang CryoSeek - Revision history