- EMDB-6272: Single particle cryo-EM structure of rotavirus VP6 at 2.6 Angstro... -
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基本情報
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データベース: EMDB / ID: EMD-6272
タイトル
Single particle cryo-EM structure of rotavirus VP6 at 2.6 Angstroms resolution
マップデータ
Unsharpened reconstruction of rotavirus VP6
試料
試料: 13-fold average of VP6 trimer from full rotavirus reconstruction
タンパク質・ペプチド: Bovine rotavirus VP6
キーワード
rotavirus / VP6 / cryo-EM / single particle
機能・相同性
機能・相同性情報
viral intermediate capsid / T=13 icosahedral viral capsid / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / viral envelope / structural molecule activity / metal ion binding 類似検索 - 分子機能
Rotavirus A/C, major capsid protein VP6 / Rotavirus major capsid protein VP6 / Virus capsid protein, alpha-helical / Viral capsid/haemagglutinin protein 類似検索 - ドメイン・相同性
Intermediate capsid protein VP6 / Intermediate capsid protein VP6 類似検索 - 構成要素
ジャーナル: Elife / 年: 2015 タイトル: Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6. 著者: Timothy Grant / Nikolaus Grigorieff / 要旨: Biological specimens suffer radiation damage when imaged in an electron microscope, ultimately limiting the attainable resolution. At a given resolution, an optimal exposure can be defined that ...Biological specimens suffer radiation damage when imaged in an electron microscope, ultimately limiting the attainable resolution. At a given resolution, an optimal exposure can be defined that maximizes the signal-to-noise ratio in the image. Using a 2.6 Å resolution single particle cryo-EM reconstruction of rotavirus VP6, determined from movies recorded with a total exposure of 100 electrons/Å(2), we obtained accurate measurements of optimal exposure values over a wide range of resolutions. At low and intermediate resolutions, our measured values are considerably higher than obtained previously for crystalline specimens, indicating that both images and movies should be collected with higher exposures than are generally used. We demonstrate a method of using our optimal exposure values to filter movie frames, yielding images with improved contrast that lead to higher resolution reconstructions. This 'high-exposure' technique should benefit cryo-EM work on all types of samples, especially those of relatively low-molecular mass.
Additional 13-fold averaging was performed on top of the I symmetry.
CTF補正
詳細: Each Particle
最終 再構成
アルゴリズム: OTHER / 解像度のタイプ: BY AUTHOR / 解像度: 2.6 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: TIGRIS, IMAGIC, FREALIGN 詳細: Final map is a 13-fold average of VP6 trimers from the asymmetric unit of the reconstruction of the whole capsid. Data at resolutions higher than 15A were not used for alignments. 使用した粒子像数: 4000