- EMDB-6328: 3D reconstruction from 188 out of 450 fibrils of Abeta(1-40), sel... -
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IDまたはキーワード:
読み込み中...
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基本情報
登録情報
データベース: EMDB / ID: EMD-6328
タイトル
3D reconstruction from 188 out of 450 fibrils of Abeta(1-40), selected by mean crossover-to-crossover distance (130 to 150 nm) and curvature (straightest 188 filaments were selected)
マップデータ
3D reconstruction of Abeta(1-40) fibril before any filtering, symmetrization, or masking. Figure 5D of the primary citation was generated from this map by application of helical symmetry and a B factor of -600A^2, with low-pass filtering to 7.5A.
ジャーナル: Proc Natl Acad Sci U S A / 年: 2008 タイトル: Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy. 著者: Carsten Sachse / Marcus Fändrich / Nikolaus Grigorieff / 要旨: Alzheimer's disease is a neurodegenerative disorder that is characterized by the cerebral deposition of amyloid fibrils formed by Abeta peptide. Despite their prevalence in Alzheimer's and other ...Alzheimer's disease is a neurodegenerative disorder that is characterized by the cerebral deposition of amyloid fibrils formed by Abeta peptide. Despite their prevalence in Alzheimer's and other neurodegenerative diseases, important details of the structure of amyloid fibrils remain unknown. Here, we present a three-dimensional structure of a mature amyloid fibril formed by Abeta(1-40) peptide, determined by electron cryomicroscopy at approximately 8-A resolution. The fibril consists of two protofilaments, each containing approximately 5-nm-long regions of beta-sheet structure. A local twofold symmetry within each region suggests that pairs of beta-sheets are formed from equivalent parts of two Abeta(1-40) peptides contained in each protofilament. The pairing occurs via tightly packed interfaces, reminiscent of recently reported steric zipper structures. However, unlike these previous structures, the beta-sheet pairing is observed within an amyloid fibril and includes significantly longer amino acid sequences.
ダウンロード / ファイル: emd_6328.map.gz / 形式: CCP4 / 大きさ: 494.2 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈
3D reconstruction of Abeta(1-40) fibril before any filtering, symmetrization, or masking. Figure 5D of the primary citation was generated from this map by application of helical symmetry and a B factor of -600A^2, with low-pass filtering to 7.5A.
ボクセルのサイズ
X=Y=Z: 1.2 Å
密度
表面レベル
登録者による: 360.0 / ムービー #1: 360
最小 - 最大
-124.848876950000005 - 910.867004390000034
平均 (標準偏差)
-1.64349163 (±56.7017746)
対称性
空間群: 1
詳細
EMDB XML:
マップ形状
Axis order
X
Y
Z
Origin
0
0
0
サイズ
510
510
510
Spacing
510
510
510
セル
A=B=C: 612.0 Å α=β=γ: 90.0 °
CCP4マップ ヘッダ情報:
mode
Image stored as Reals
Å/pix. X/Y/Z
1.2
1.2
1.2
M x/y/z
510
510
510
origin x/y/z
0.000
0.000
0.000
length x/y/z
612.000
612.000
612.000
α/β/γ
90.000
90.000
90.000
MAP C/R/S
1
2
3
start NC/NR/NS
0
0
0
NC/NR/NS
510
510
510
D min/max/mean
-124.849
910.867
-1.643
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添付データ
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試料の構成要素
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全体 : human Abeta(1-40)
全体
名称: human Abeta(1-40)
要素
試料: human Abeta(1-40)
タンパク質・ペプチド: Amyloid beta peptide (1-40)
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超分子 #1000: human Abeta(1-40)
超分子
名称: human Abeta(1-40) / タイプ: sample / ID: 1000 / 集合状態: Helical assembly / Number unique components: 1
Filaments were processed using Frealix, including restraints on all refinement parameters. Data up to 20A were used in early stages of refinement. This limit was gradually increased to 9A.
最終 再構成
想定した対称性 - らせんパラメータ - Δz: 4.8 Å 想定した対称性 - らせんパラメータ - ΔΦ: 0.734 ° 想定した対称性 - らせんパラメータ - 軸対称性: C2 (2回回転対称) アルゴリズム: OTHER / 解像度のタイプ: BY AUTHOR / 解像度: 7.1 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: Frealix 詳細: Data up to 20A were used in early stages of the refinement. This limit was gradually increased to 9A.