+データを開く
-基本情報
登録情報 | データベース: SASBDB / ID: SASDBJ3 |
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試料 | Bovine serum albumin, monomer from SEC-SAXS
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機能・相同性 | 機能・相同性情報 enterobactin binding / cellular response to calcium ion starvation / negative regulation of mitochondrial depolarization / toxic substance binding / cellular response to starvation / fatty acid binding / pyridoxal phosphate binding / protein-containing complex / DNA binding / extracellular space ...enterobactin binding / cellular response to calcium ion starvation / negative regulation of mitochondrial depolarization / toxic substance binding / cellular response to starvation / fatty acid binding / pyridoxal phosphate binding / protein-containing complex / DNA binding / extracellular space / extracellular region / metal ion binding / cytoplasm 類似検索 - 分子機能 |
生物種 | Bos taurus (ウシ) |
引用 | ジャーナル: Nat Protoc / 年: 2016 タイトル: Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments. 著者: Cy M Jeffries / Melissa A Graewert / Clément E Blanchet / David B Langley / Andrew E Whitten / Dmitri I Svergun / 要旨: Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) are techniques used to extract structural parameters and determine the overall structures and shapes of biological ...Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) are techniques used to extract structural parameters and determine the overall structures and shapes of biological macromolecules, complexes and assemblies in solution. The scattering intensities measured from a sample contain contributions from all atoms within the illuminated sample volume, including the solvent and buffer components, as well as the macromolecules of interest. To obtain structural information, it is essential to prepare an exactly matched solvent blank so that background scattering contributions can be accurately subtracted from the sample scattering to obtain the net scattering from the macromolecules in the sample. In addition, sample heterogeneity caused by contaminants, aggregates, mismatched solvents, radiation damage or other factors can severely influence and complicate data analysis, so it is essential that the samples be pure and monodisperse for the duration of the experiment. This protocol outlines the basic physics of SAXS and SANS, and it reveals how the underlying conceptual principles of the techniques ultimately 'translate' into practical laboratory guidance for the production of samples of sufficiently high quality for scattering experiments. The procedure describes how to prepare and characterize protein and nucleic acid samples for both SAXS and SANS using gel electrophoresis, size-exclusion chromatography (SEC) and light scattering. Also included are procedures that are specific to X-rays (in-line SEC-SAXS) and neutrons, specifically preparing samples for contrast matching or variation experiments and deuterium labeling of proteins. |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #447 | タイプ: atomic / ダミー原子の半径: 1.90 A / カイ2乗値: 0.945 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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モデル #449 | タイプ: dummy / ダミー原子の半径: 2.50 A / カイ2乗値: 0.972196 / P-value: 0.173000 Omokage検索でこの集合体の類似形状データを探す (詳細) |
-試料
試料 | 名称: Bovine serum albumin, monomer from SEC-SAXS |
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バッファ | 名称: 25 mM Tris 150 mM NaCl 3% (v/v) glycerol / 濃度: 25.00 mM / pH: 7.5 / 組成: 150 mM NaCl 3% v/v glycerol |
要素 #298 | 名称: BSA monomer / タイプ: protein / 記述: Bovine serum albumin, monomer / 分子量: 66.462 / 分子数: 1 / 由来: Bos taurus / 参照: UniProt: P02769 配列: DTHKSEIAHR FKDLGEEHFK GLVLIAFSQY LQQCPFDEHV KLVNELTEFA KTCVADESHA GCEKSLHTLF GDELCKVASL RETYGDMADC CEKQEPERNE CFLSHKDDSP DLPKLKPDPN TLCDEFKADE KKFWGKYLYE IARRHPYFYA PELLYYANKY NGVFQECCQA ...配列: DTHKSEIAHR FKDLGEEHFK GLVLIAFSQY LQQCPFDEHV KLVNELTEFA KTCVADESHA GCEKSLHTLF GDELCKVASL RETYGDMADC CEKQEPERNE CFLSHKDDSP DLPKLKPDPN TLCDEFKADE KKFWGKYLYE IARRHPYFYA PELLYYANKY NGVFQECCQA EDKGACLLPK IETMREKVLT SSARQRLRCA SIQKFGERAL KAWSVARLSQ KFPKAEFVEV TKLVTDLTKV HKECCHGDLL ECADDRADLA KYICDNQDTI SSKLKECCDK PLLEKSHCIA EVEKDAIPEN LPPLTADFAE DKDVCKNYQE AKDAFLGSFL YEYSRRHPEY AVSVLLRLAK EYEATLEECC AKDDPHACYS TVFDKLKHLV DEPQNLIKQN CDQFEKLGEY GFQNALIVRY TRKVPQVSTP TLVEVSRSLG KVGTRCCTKP ESERMPCTED YLSLILNRLC VLHEKTPVSE KVTKCCTESL VNRRPCFSAL TPDETYVPKA FDEKLFTFHA DICTLPDTEK QIKKQTALVE LLKHKPKATE EQLKTVMENF VAFVDKCCAA DDKEACFAVE GPKLVVSTQT ALA |
-実験情報
ビーム | 設備名称: PETRA III EMBL P12 / 地域: Hamburg / 国: Germany / 線源: X-ray synchrotron / 波長: 0.12 Å / スペクトロメータ・検出器間距離: 3.1 mm | |||||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus 2M | |||||||||||||||||||||||||||||||||
スキャン | タイトル: Bovine serum albumin, monomer / 測定日: 2014年1月23日 / 保管温度: 20 °C / 照射時間: 1 sec. / フレーム数: 3500 / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 4.6 / ポイント数: 395 /
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結果 | カーブのタイプ: other /
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