7xhr

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Crystal structure of Wild Type Cypovirus Polyhedra produced by cell-free protein synthesisCrystal structure of Wild Type Cypovirus Polyhedra produced by cell-free protein synthesis

Structural highlights

7xhr is a 1 chain structure with sequence from Bombyx mori cypovirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.801Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYHD_CPVBM Major component of the virus occlusion bodies, which are large proteinaceous structures (polyhedra), that protect the virus from the outside environment for extended periods until they are ingested by insect larvae.

Publication Abstract from PubMed

In-cell protein crystallization (ICPC) has been investigated as a technique to support the advancement of structural biology because it does not require protein purification and a complicated crystallization process. However, only a few protein structures have been reported because these crystals formed incidentally in living cells and are insufficient in size and quality for structure analysis. Here, we have developed a cell-free protein crystallization (CFPC) method, which involves direct protein crystallization using cell-free protein synthesis. We have succeeded in crystallization and structure determination of nano-sized polyhedra crystal (PhC) at a high resolution of 1.80 A. Furthermore, nanocrystals were synthesized at a reaction scale of only 20 muL using the dialysis method, enabling structural analysis at a resolution of 1.95 A. To further demonstrate the potential of CFPC, we attempted to determine the structure of crystalline inclusion protein A (CipA), whose structure had not yet been determined. We added chemical reagents as a twinning inhibitor to the CFPC solution, which enabled us to determine the structure of CipA at 2.11 A resolution. This technology greatly expands the high-throughput structure determination method of unstable, low-yield, fusion, and substrate-biding proteins that have been difficult to analyze with conventional methods.

Cell-free protein crystallization for nanocrystal structure determination.,Abe S, Tanaka J, Kojima M, Kanamaru S, Hirata K, Yamashita K, Kobayashi A, Ueno T Sci Rep. 2022 Oct 3;12(1):16031. doi: 10.1038/s41598-022-19681-9. PMID:36192567[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Abe S, Tanaka J, Kojima M, Kanamaru S, Hirata K, Yamashita K, Kobayashi A, Ueno T. Cell-free protein crystallization for nanocrystal structure determination. Sci Rep. 2022 Oct 3;12(1):16031. doi: 10.1038/s41598-022-19681-9. PMID:36192567 doi:http://dx.doi.org/10.1038/s41598-022-19681-9

7xhr, resolution 1.80Å

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