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4S1K

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

4S1K の概要
エントリーDOI10.2210/pdb4s1k/pdb
関連するPDBエントリー4S1L
分子名称Polyhedrin, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
機能のキーワードpolyhedrin, viral protein
由来する生物種Uranotaenia sapphirina cypovirus
タンパク質・核酸の鎖数1
化学式量合計27479.00
構造登録者
主引用文献Ginn, 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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 4s1k
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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