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データを開く
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基本情報
| 登録情報 | データベース: PDB / ID: 1wtn | ||||||
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| タイトル | The structure of HEW Lysozyme Orthorhombic Crystal Growth under a High Magnetic Field | ||||||
要素 | Lysozyme C | ||||||
キーワード | HYDROLASE / Allergen | ||||||
| 機能・相同性 | 機能・相同性情報Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium ...Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm 類似検索 - 分子機能 | ||||||
| 生物種 | ![]() | ||||||
| 手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 1.13 Å | ||||||
データ登録者 | Saijo, S. / Yamada, Y. / Sato, T. / Tanaka, N. / Matsui, T. / Sazaki, G. / Nakajima, K. / Matsuura, Y. | ||||||
引用 | ジャーナル: Acta Crystallogr.,Sect.D / 年: 2005タイトル: Structural consequences of hen egg-white lysozyme orthorhombic crystal growth in a high magnetic field: validation of X-ray diffraction intensity, conformational energy searching and ...タイトル: Structural consequences of hen egg-white lysozyme orthorhombic crystal growth in a high magnetic field: validation of X-ray diffraction intensity, conformational energy searching and quantitative analysis of B factors and mosaicity. 著者: Saijo, S. / Yamada, Y. / Sato, T. / Tanaka, N. / Matsui, T. / Sazaki, G. / Nakajima, K. / Matsuura, Y. | ||||||
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構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 1wtn.cif.gz | 40.1 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb1wtn.ent.gz | 27.8 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 1wtn.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/wt/1wtn ftp://data.pdbj.org/pub/pdb/validation_reports/wt/1wtn | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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| 単位格子 |
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要素
| #1: タンパク質 | 分子量: 14331.160 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
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| #2: 化合物 | ChemComp-CL / |
| #3: 水 | ChemComp-HOH / |
| Has protein modification | Y |
-実験情報
-実験
| 実験 | 手法: X線回折 / 使用した結晶の数: 8 |
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試料調製
| 結晶 | マシュー密度: 2.27 Å3/Da / 溶媒含有率: 45.81 % |
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| 結晶化 | 温度: 313 K / 手法: under a high magnetic field of 10t / pH: 4.5 詳細: NaCl, sodium acetate, pH 4.5, under a High Magnetic Field of 10T, temperature 313K |
-データ収集
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| 放射光源 |
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| 検出器 |
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| 放射 | モノクロメーター: Si 111 / プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray | |||||||||||||||
| 放射波長 | 波長: 1 Å / 相対比: 1 | |||||||||||||||
| 反射 | 解像度: 1.13→50 Å / Num. all: 34622 / Num. obs: 34449 / % possible obs: 99.5 % / Observed criterion σ(I): 3 | |||||||||||||||
| 反射 シェル | 解像度: 1.13→1.16 Å / % possible all: 71.9 |
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解析
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| 精密化 | 構造決定の手法: 分子置換 / 解像度: 1.13→16 Å / σ(F): 3 詳細: technically defined here as 10 T and 0 T crystals, were grown by exposing them to a high magnetic field of 10 T (this entry 1WTN) and a control geomagnetic field of 40 uT(entry 1WTM), ...詳細: technically defined here as 10 T and 0 T crystals, were grown by exposing them to a high magnetic field of 10 T (this entry 1WTN) and a control geomagnetic field of 40 uT(entry 1WTM), respectively (Sato,T., Yamada,Y., Saijo,S., Hori,T., Hirose,R., Tanaka,N., Sazaki,G., Nakajima,K., Igarashi,N., Tanaka,M. & Matsuura,Y. (2000). Acta Cryst. D56, 1079-1083.). A continuous homogeneous magnetic field of 10 T was produced by a liquid helium-free superconducting magnet (JMTD-10T100M9) (Japan Magnetic Technology Inc., Tokyo, Japan). Orthorhombic lysozyme crystals were grown, in the high magnetic field, via the batch crystallization method. The crystal growth conditions were 250 mg.ml-1 lysozyme, 42 mM NaCl in 50 mM sodium acetate buffer with pH 4.5 at 313 K; 11 days duration. The dimensions of the 10 T and 0 T crystals were typically 0.45 X 0.50 X 2.00 and 0.50 X 0.50 X 2.00 mm, respectively. The starting model for molecular replacement in each case was the refined atomic coordinates (entry 1BGI) of the HEW lysozyme obtained from the PDB (Oki,H., Matsuura,Y., Komatsu,H. & Chernov,A.A. (1999). Acta Cryst. D55, 114- 121.), i.e., our best resolution structure for the orthorhombic lysozyme refined so far (at 1.7 A resolution).
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| Refine analyze | Luzzati coordinate error obs: 0.16 Å | ||||||||||||
| 精密化ステップ | サイクル: LAST / 解像度: 1.13→16 Å
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| 拘束条件 |
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