+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-21513 | |||||||||
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タイトル | Pig Ryanodine Receptor (WT) in 5mM EGTA condition | |||||||||
マップデータ | Final map from cryoSPARC | |||||||||
試料 |
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キーワード | receptor / calcium / channel / complex / TRANSPORT PROTEIN-ISOMERASE complex | |||||||||
機能・相同性 | 機能・相同性情報 positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / response to redox state / protein maturation by protein folding / 'de novo' protein folding ...positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / response to redox state / protein maturation by protein folding / 'de novo' protein folding / negative regulation of heart rate / FK506 binding / positive regulation of axon regeneration / channel regulator activity / smooth muscle contraction / response to vitamin E / calcium channel inhibitor activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / T cell proliferation / Ion homeostasis / release of sequestered calcium ion into cytosol / regulation of cytosolic calcium ion concentration / sarcoplasmic reticulum membrane / calcium channel complex / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / calcium-mediated signaling / response to hydrogen peroxide / Stimuli-sensing channels / Z disc / positive regulation of cytosolic calcium ion concentration / protein refolding / transmembrane transporter binding / signaling receptor binding / membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | Sus scrofa (ブタ) / Homo sapiens (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.0 Å | |||||||||
データ登録者 | Woll KW / Haji-Ghassemi O | |||||||||
資金援助 | 1件
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引用 | ジャーナル: Nat Commun / 年: 2021 タイトル: Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM. 著者: Kellie A Woll / Omid Haji-Ghassemi / Filip Van Petegem / 要旨: Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and ...Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and arrhythmias. Here, we explore the first MH mutation identified in humans by providing cryo-EM snapshots of the pig homolog, R615C, showing that it affects an interface between three solenoid regions. We also show the impact of apo-calmodulin (apoCaM) and how it can induce opening by bending of the bridging solenoid, mediated by its N-terminal lobe. For R615C RyR1, apoCaM binding abolishes a pathological 'intermediate' conformation, distributing the population to a mixture of open and closed channels, both different from the structure without apoCaM. Comparisons show that the mutation primarily affects the closed state, inducing partial movements linked to channel activation. This shows that disease mutations can cause distinct pathological conformations of the RyR and facilitate channel opening by disrupting interactions between different solenoid regions. | |||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_21513.map.gz | 398.6 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-21513-v30.xml emd-21513.xml | 25.1 KB 25.1 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_21513.png | 200.6 KB | ||
Filedesc metadata | emd-21513.cif.gz | 8.6 KB | ||
その他 | emd_21513_additional_1.map.gz emd_21513_additional_2.map.gz emd_21513_half_map_1.map.gz emd_21513_half_map_2.map.gz | 38.4 MB 57.5 MB 390.4 MB 390.4 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-21513 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21513 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_21513_validation.pdf.gz | 165 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_21513_full_validation.pdf.gz | 164.5 KB | 表示 | |
XML形式データ | emd_21513_validation.xml.gz | 497 B | 表示 | |
CIF形式データ | emd_21513_validation.cif.gz | 373 B | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21513 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21513 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_21513.map.gz / 形式: CCP4 / 大きさ: 421.9 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Final map from 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: 1.37083 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
-追加マップ: Density modified map obtained from PHENIX Resolve
ファイル | emd_21513_additional_1.map | ||||||||||||
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注釈 | Density modified map obtained from PHENIX Resolve | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-追加マップ: composite map made from focused (masked) refinements conducted...
ファイル | emd_21513_additional_2.map | ||||||||||||
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注釈 | composite map made from focused (masked) refinements conducted in RELION | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_21513_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #2
ファイル | emd_21513_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
-全体 : ryanodine receptor-FKBP1B complex
全体 | 名称: ryanodine receptor-FKBP1B complex |
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要素 |
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-超分子 #1: ryanodine receptor-FKBP1B complex
超分子 | 名称: ryanodine receptor-FKBP1B complex / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#2 |
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-超分子 #2: ryanodine receptor
超分子 | 名称: ryanodine receptor / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: #2 |
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由来(天然) | 生物種: Sus scrofa (ブタ) |
-超分子 #3: FKBP1B
超分子 | 名称: FKBP1B / タイプ: complex / ID: 3 / 親要素: 1 / 含まれる分子: #1 |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-分子 #1: Peptidyl-prolyl cis-trans isomerase FKBP1B
分子 | 名称: Peptidyl-prolyl cis-trans isomerase FKBP1B / タイプ: protein_or_peptide / ID: 1 / コピー数: 4 / 光学異性体: LEVO / EC番号: peptidylprolyl isomerase |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 11.939562 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: SNAGVEIETI SPGDGRTFPK KGQTCVVHYT GMLQNGKKFD SSRDRNKPFK FRIGKQEVIK GFEEGAAQMS LGQRAKLTCT PDVAYGATG HPGVIPPNAT LIFDVELLNL E UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B |
-分子 #2: Ryanodine Receptor
分子 | 名称: Ryanodine Receptor / タイプ: protein_or_peptide / ID: 2 / コピー数: 4 / 光学異性体: LEVO |
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由来(天然) | 生物種: Sus scrofa (ブタ) |
分子量 | 理論値: 510.786406 KDa |
配列 | 文字列: MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP DLAICCFVLE QSLSVRALQE MLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSGMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT THPASKQRSE G EKVRVGDD ...文字列: MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP DLAICCFVLE QSLSVRALQE MLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSGMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT THPASKQRSE G EKVRVGDD LILVSVSSER YLHLSTASGE LQVDASFMQT LWNMNPICSG CEEGYVTGGH VLRLFHGHMD ECLTISPADS DD QRRLVYY EGGSVCTHAR SLWRLEPLRI SWSGSHLRWG QPLRIRHVTT GRYLALIEDQ GLVVVDASKA HTKATSFCFR ISK EKLDTA PKRDVEGMGP PEIKYGESLC FVQHVASGLW LTYAAPDPKA LRLGVLKKKA ILHQEGHMDD ALSLTRCQQE ESQA ARMIY STAGLYNHFI KGLDSFSGKP RGSGAPAGTA LPLEGVILSL QDLIGYFEPP SEELQHEEKQ SKLRSLRNRQ SLFQE EGML SLVLNCIDRL NVYTTAAHFA EFAGEEAAES WKEIVNLLYE ILASLIRGNR ANCALFSNNL DWLVSKLDRL EASSGI LEV LYCVLIESPE VLNIIQENHI KSIISLLDKH GRNHKVLDVL CSLCVCNGVA VRSNQDLITE NLLPGRELLL QTNLINY VT SIRPNIFVGR AEGTTQYSKW YFEVMVDEVV PFLTAQATHL RVGWALTEGY SPYPGGGEGW GGNGVGDDLY SYGFDGLH L WTGHVPRLVT SPGQHLLAPE DVVSCCLDLS VPSISFRING CPVQGVFEAF NLNGLFFPVV SFSAGVKVRF LLGGRHGEF KFLPPPGYAP CHEAVLPRER LRLEPIKEYR REGPRGPHLV GPSRCLSHTD FVPCPVDTVQ IVLPPHLERI REKLAENIHE LWALTRIEQ GWTYGPVRDD NKRLHPCLVD FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN LRKTKLPKTY M MSNGYKPA PLDLSHVRLT PAQTTLVDRL AENGHNVWAR DRVAQGWSYS AVQDIPARRN PRLVPYRLLD EATKRSNRDS LC QAVRTLL GYGYNIEPPD QEPSQVESQS RWDRVRIFRA EKSYAVQSGR WYFEFEAVTT GEMRVGWARP ELRPDVELGA DEL AYVFNG HRGQRWHLGS ELFGRPWQSG DVVGCMIDLT ENTIIFTLNG EVLMSDSGSE TAFRDIEVGD GFLPVCSLGP GQVG HLNLG QDVSSLRFFA ICGLQEGFEP FAINMQRPVT TWFSKSLPQF EAVPLEHPHY EVSRVDGTVD TPPCLRLTHR TWGSQ NSLV EMLFLRLSLP VQFHQHFRCT AGATPLAPPG LQPPAEDEAR AAEPDPDYEN LRRSAGRWGE AEGGKEGTAK EGAPGG TAQ AGVEAQPPRA ENEKDATTEK NKKRGFLFKA KKAAMMTQPP ATPTLPRLPH EVVPADDRDD PDIILNTTTY YYSVRVF AG QEPSCVWVGW VTPDYHQHDM NFDLTKVRAV TVTMGDEQGN IHSSLKCSNC YMVWGGDFVS PGQQGRISHT DLVIGCLV D LATGLMTFTA NGKESNTFFQ VEPNTKLFPA VFVLPTHQNV IQFELGKQKN IMPLSAAMFL SERKNPAPQC PPRLEMQML MPVSWSRMPN HFLRVETRRA GERLGWAVQC QEPLTMMALH IPEENRCMDI LELSERLDLQ QFHSHTLRLY RAVCALGNNR VAHALCSHV DQAQLLHALE DAHLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT PETRAITLFP PGKRTENGPR R HGLPGVGV TTSLRPPHHF SAPCFVAALP AVGAAEAPAR LSPSIPLEAL RDKALRMLGE AVRDGGQHAR DPVGGSVEFQ FV PVLKLVS TLLVMGIFGD EDVKQILKMI EPEVFTEEEE EEEEEEEEEE EDEEEKEEDE EEEAREKEDE EKEEEETAEG EKE EYLEEG LLQMKLPESV KLQMCNLLEY FCDQELQHRV ESLAAFAERY VDKLQANQRD RYGILMKAFT MTAAETARRT REFR SPPQE QINMLLHFKD GEDEEDCPLP DEIRQDLLEF HQDLLTHCGI QLEGEEEEPE EEATLGSRLM SLLEKVRLVK KKEEK SEEE PPAEESKLQS LQELVSHTVV RWAQEDFVQS PELVRAMFSL LHRQYDGLGE LLRALPRAYT ISPSSVEDTM SLLECL GQI RSLLIVQMGP QEENLMIQSI GNIMNNKVFY QHPNLMRALG MHETVMEVMV NVLGGGESKE IRFPKMVTSC CRFLCYF CR ISRQNQRSMF DHLSYLLENS GIGLGMQGST PLDVAAASVI DNNELALALQ EQDLEKVVSY LAGCGLQSCP MLLAKGYP D IGWNPCGGER YLDFLRFAVF VNGESVEENA NVVVRLLIRK PECFGPALRG EGGSGLLATI EEAIRISEDP ARDGPGVRR DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE MHLIQAGKGE ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQP KMSASFVPDH KASMVLFLDR VYGIENQDFL LHVLDVGFLP DMRAAASLDT ATFSTTEMAL ALNRYLCLAV L PLITKCAP LFAGTEHRAI MVDSMLHTVY RLSRGRSLTK AQRDVIEECL MALCRYIRPS MLQHLLRRLV FDVP(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)DPRPVET LNVIIPEK L DSFINKFAEY THEKWAFDKI QNNWSYGENI DEELKTHPML RPYKTFSEKD KEIYRWPIKE SLKAMIAWEW TIEKAREGE EEKTEKKKTR KISQSAQTYD AREGYNPQPP DLSGVTLSRE LQAMAEQLAE NYHNTWGRKK KQELEAKGGG THPLLVPYDT LTAKEKARD REKAQELLKF LQMNGYAVTR (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)PLLIRYV DNNRAHWLTE PNPSAEELFR MVGEIFIYWS K(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) SLRWQMALYR GLPGREEDA DDPEKIVRRV QEVSAVLYHL EQMEHPYKSK (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)MTPLYNLP THRACNM FL ESYKAAWILT EDHSFEDRMI DDLSKAGEQE EEEEEVEEKK PDPLHQLVLH FSRTALTEKS KLDEDYLYMA YADIMAKS C HLEEGGENGE AQEEVEVSFE EKEMEKQRLL YQQARLHNRG AAEMVLQMIS ACKGETGAMV SSTLKLGISI LNGGNADVQ QKMLDYLKDK KEVGFFQSIQ ALMQTCSVLD LNAFERQNKA EGLGMVNEDG TVINRQNGEK VMADDEFTQD LFRFLQLLCE GHNNDFQNY LRTQTGNTTT INIIICTVDY LLRLQESISD FYWYYSGKDV IEEQGKRNFS KAMSVAKQVF NSLTEYIQGP C TGNQQSLA HSRLWDAVVG FLHVFAHMMM KLAQDSSQIE LLKELLDLQK DMVVMLLSLL EGNVVNGMIA RQMVDMLVES SS NVEMILK FFDMFLKLKD IVGSEAFQDY VTDPRGLISK KDFQK(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)EEFANRFQ EPARDIGFNV AVLLTNLSEH VPHDPRLRNF LELAESILEY FRPYLGRIEI MGASRRIERI YFEISETNRA QWEMPQVKES KRQFIFDVV NEGGESEKME LFVSFCEDTI FEMQIAAQIS EPEGEPEEDE DEGAGLAEAG AEGAEEGAVG PEGAAGTAAA G LTARLAAA TSRALRGLSY RSLRRRVRRL RRLTAREAAT ALAALLWAAL AHAGAAGAGA AAGALRLLWG SLFGGGLVEG AK KVTVTEL LAGMPDPTGD EVHGEQPAGP GGEADGEGAG EGAGEAWEGA GDEEVAVQEA GPGGADGAVA VAEGGPFRPE GAG GLGDMG DTTPAEPPTP EGSPIIKRKL GVDGEEEELP PEPEPEPEPE PEKADAENGE KEEVPKPPPE PPKKTAPPPP PPKK EEGGS GGLEFWGELE VQRVKFLNYL SRNFYTLRFL ALFLAFAINF ILLFYKVSDS PPGEDDMEGS AAGDLSGAGS GGGSG WGSG AGEEVEGDED ENMVYYFLEE STGYMEPALR CLSLLHTLVA FLCIIGYNCL KVPLVIFKRE KELARKLEFD GLYITE QPE DDDVKGQWDR LVLNTPSFPS NYWDKFVKRK VLDKHGDIYG RERIAELLGM DLATLEITAH NERKPEPPPG LLTWLMS ID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYL Y TVVAFNFFRK FYNKSEDEDE PDMKCDDMMT CYLFHMYVGV RAGGGIGDEI EDPAGDEYEL YRVVFDITFF FFVIVILLA IIQGLIIDAF GELRDQQEQV REDMETKCFI CGIGSDYFDT TPHRFETHTL EEHNLANYMF FLMYLINKDE TEHTGQESYV WKMYQERCW DFFPAGDCFR KQYEDQLS |
-分子 #3: ZINC ION
分子 | 名称: ZINC ION / タイプ: ligand / ID: 3 / コピー数: 4 / 式: ZN |
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分子量 | 理論値: 65.409 Da |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.5 |
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グリッド | 材質: GRAPHENE OXIDE |
凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 平均電子線量: 30.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: OTHER / 撮影モード: DIFFRACTION |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
-画像解析
初期モデル | モデルのタイプ: PDB ENTRY |
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最終 再構成 | 想定した対称性 - 点群: C4 (4回回転対称) / 解像度のタイプ: BY AUTHOR / 解像度: 4.0 Å / 解像度の算出法: FSC 0.143 CUT-OFF / ソフトウェア - 名称: PHENIX (ver. dev-3714) / 使用した粒子像数: 52289 |
初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |