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データを開く
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基本情報
登録情報 | ![]() | |||||||||||||||
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タイトル | Structure of a ribosome with tethered subunits | |||||||||||||||
![]() | Cryo-EM structure of the RiboTv3 tethered ribosome. Raw micrograph acquisition was done with a Talos Arctica (200kV) microscope at 100,000X magnification. Map generation was done with CryoSPARC. | |||||||||||||||
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![]() | Engineered / Tethered / Synthetic / RIBOSOME | |||||||||||||||
機能・相同性 | ![]() DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / small ribosomal subunit ...DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / small ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / response to antibiotic / mRNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||||||||
生物種 | ![]() ![]() ![]() ![]() | |||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.18 Å | |||||||||||||||
![]() | Kim DS / Watkins A / Bidstrup E / Lee J / Topkar VV / Kofman C / Schwarz KJ / Liu Y / Pintilie G / Roney E ...Kim DS / Watkins A / Bidstrup E / Lee J / Topkar VV / Kofman C / Schwarz KJ / Liu Y / Pintilie G / Roney E / Das R / Jewett MC | |||||||||||||||
資金援助 | ![]()
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![]() | ジャーナル: Acta Crystallogr D Struct Biol / 年: 2019 タイトル: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. 著者: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / ...著者: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / ![]() ![]() ![]() 要旨: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks. #1: ![]() タイトル: UCSF ChimeraX: Structure visualization for researchers, educators, and developers. 著者: Pettersen EF / Goddard TD / Huang CC / Meng EC / Couch GS / Croll TI / Morris JH / Ferrin TE #2: ![]() タイトル: cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. 著者: Punjani A / Rubinstein JL / Fleet DJ / Brubaker MA | |||||||||||||||
履歴 |
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構造の表示
添付画像 |
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ダウンロードとリンク
-EMDBアーカイブ
マップデータ | ![]() | 236.1 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 83.5 KB 83.5 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 17.4 KB | 表示 | ![]() |
画像 | ![]() | 216.8 KB | ||
Filedesc metadata | ![]() | 16.3 KB | ||
その他 | ![]() ![]() | 441.9 MB 441.9 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 1.2 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.2 MB | 表示 | |
XML形式データ | ![]() | 25.2 KB | 表示 | |
CIF形式データ | ![]() | 32.9 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 7uphMC M: このマップから作成された原子モデル C: 同じ文献を引用 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||
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注釈 | Cryo-EM structure of the RiboTv3 tethered ribosome. Raw micrograph acquisition was done with a Talos Arctica (200kV) microscope at 100,000X magnification. Map generation was done with CryoSPARC. | ||||||||||||||||||||||||||||||||||||
投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-ハーフマップ: D 1000263105 em-volume Half Map A
ファイル | emd_26666_half_map_1.map | ||||||||||||
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注釈 | D_1000263105_em-volume Half Map A | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: D 1000263105 em-volume Half Map B
ファイル | emd_26666_half_map_2.map | ||||||||||||
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注釈 | D_1000263105_em-volume Half Map B | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : Ribosome with tethered subunits
+超分子 #1: Ribosome with tethered subunits
+分子 #1: 30S ribosomal protein S14
+分子 #2: 30S ribosomal protein S15
+分子 #3: 30S ribosomal protein S16
+分子 #4: 30S ribosomal protein S17
+分子 #5: 30S ribosomal protein S18
+分子 #6: 30S ribosomal protein S19
+分子 #7: 30S ribosomal protein S20
+分子 #8: 30S ribosomal protein S21
+分子 #11: 50S ribosomal protein L2
+分子 #12: 50S ribosomal protein L3
+分子 #13: 50S ribosomal protein L4
+分子 #14: 50S ribosomal protein L5
+分子 #15: 50S ribosomal protein L6
+分子 #16: 50S ribosomal protein L13
+分子 #17: 50S ribosomal protein L14
+分子 #18: 50S ribosomal protein L15
+分子 #19: 50S ribosomal protein L16
+分子 #20: 50S ribosomal protein L17
+分子 #21: 30S ribosomal protein S2
+分子 #22: 30S ribosomal protein S3
+分子 #23: 30S ribosomal protein S4
+分子 #24: 30S ribosomal protein S5
+分子 #25: 30S ribosomal protein S6
+分子 #26: 30S ribosomal protein S7
+分子 #27: 30S ribosomal protein S8
+分子 #28: 30S ribosomal protein S9
+分子 #29: 30S ribosomal protein S10
+分子 #30: 30S ribosomal protein S11
+分子 #31: 30S ribosomal protein S12
+分子 #32: 30S ribosomal protein S13
+分子 #33: 50S ribosomal protein L32
+分子 #34: 50S ribosomal protein L33
+分子 #35: 50S ribosomal protein L34
+分子 #36: 50S ribosomal protein L35
+分子 #37: 50S ribosomal protein L36
+分子 #38: 50S ribosomal protein L18
+分子 #39: 50S ribosomal protein L19
+分子 #40: 50S ribosomal protein L20
+分子 #41: 50S ribosomal protein L21
+分子 #42: 50S ribosomal protein L22
+分子 #43: 50S ribosomal protein L23
+分子 #44: 50S ribosomal protein L24
+分子 #45: 50S ribosomal protein L25
+分子 #46: 50S ribosomal protein L27
+分子 #47: 50S ribosomal protein L28
+分子 #48: 50S ribosomal protein L29
+分子 #49: 50S ribosomal protein L30
+分子 #9: Tethered rRNA
+分子 #10: 5S rRNA
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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グリッド | モデル: Quantifoil R2/1 / 材質: COPPER / 前処理 - タイプ: GLOW DISCHARGE |
凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | TFS TALOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均露光時間: 1.35 sec. / 平均電子線量: 50.0 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: ![]() |
電子光学系 | 照射モード: SPOT SCAN / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.2 µm / 最小 デフォーカス(公称値): 1.2 µm |