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4S1K

Structure of Uranotaenia sapphirina cypovirus (CPV17) polyhedrin at 100 K

Summary for 4S1K
Entry DOI10.2210/pdb4s1k/pdb
Related4S1L
DescriptorPolyhedrin, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordspolyhedrin, viral protein
Biological sourceUranotaenia sapphirina cypovirus
Total number of polymer chains1
Total formula weight27479.00
Authors
Primary citationGinn, H.M.,Messerschmidt, M.,Ji, X.,Zhang, H.,Axford, D.,Gildea, R.J.,Winter, G.,Brewster, A.S.,Hattne, J.,Wagner, A.,Grimes, J.M.,Evans, G.,Sauter, N.K.,Sutton, G.,Stuart, D.I.
Structure of CPV17 polyhedrin determined by the improved analysis of serial femtosecond crystallographic data.
Nat Commun, 6:6435-6435, 2015
Cited by
PubMed Abstract: The X-ray free-electron laser (XFEL) allows the analysis of small weakly diffracting protein crystals, but has required very many crystals to obtain good data. Here we use an XFEL to determine the room temperature atomic structure for the smallest cytoplasmic polyhedrosis virus polyhedra yet characterized, which we failed to solve at a synchrotron. These protein microcrystals, roughly a micron across, accrue within infected cells. We use a new physical model for XFEL diffraction, which better estimates the experimental signal, delivering a high-resolution XFEL structure (1.75 Å), using fewer crystals than previously required for this resolution. The crystal lattice and protein core are conserved compared with a polyhedrin with less than 10% sequence identity. We explain how the conserved biological phenotype, the crystal lattice, is maintained in the face of extreme environmental challenge and massive evolutionary divergence. Our improved methods should open up more challenging biological samples to XFEL analysis.
PubMed: 25751308
DOI: 10.1038/ncomms7435
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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数据于2025-07-30公开中

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