EMDB-47378: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dime...

基本情報

登録情報

データベース: EMDB / ID: EMD-47378

• タイトル: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Nde1-Lis1 condition
• マップデータ: Sharpened map for for dimeric motor domains of phi-like dynein-1 bound to a Lis1 dimer under Nde1_Lis1 condition

試料

• 複合体: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Nde1-Lis1 condition
  • タンパク質・ペプチド: Cytoplasmic dynein 1 heavy chain 1
  • タンパク質・ペプチド: Platelet-activating factor acetylhydrolase IB subunit beta
• リガンド: ADENOSINE-5'-DIPHOSPHATE
• リガンド: ADENOSINE-5'-TRIPHOSPHATE
• リガンド: MAGNESIUM ION

• キーワード: dynein-1 / phi-like conformation / Lis1 / MOTOR PROTEIN

機能・相同性

分子機能:

corpus callosum morphogenesis / microtubule cytoskeleton organization involved in establishment of planar polarity / ameboidal-type cell migration / establishment of planar polarity of embryonic epithelium / 1-alkyl-2-acetylglycerophosphocholine esterase complex / maintenance of centrosome location / platelet activating factor metabolic process / radial glia-guided pyramidal neuron migration / acrosome assembly / central region of growth cone / cerebral cortex neuron differentiation / establishment of centrosome localization / microtubule sliding / positive regulation of embryonic development / positive regulation of cytokine-mediated signaling pathway / microtubule organizing center organization / interneuron migration / layer formation in cerebral cortex / auditory receptor cell development / nuclear membrane disassembly / astral microtubule / positive regulation of dendritic spine morphogenesis / cortical microtubule organization / positive regulation of intracellular transport / myeloid leukocyte migration / reelin-mediated signaling pathway / regulation of metaphase plate congression / establishment of spindle localization / positive regulation of spindle assembly / stereocilium / osteoclast development / microtubule plus-end binding / brain morphogenesis / vesicle transport along microtubule / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / retrograde axonal transport / kinesin complex / minus-end-directed microtubule motor activity / P-body assembly / negative regulation of JNK cascade / microtubule associated complex / dynein light intermediate chain binding / cytoplasmic dynein complex / motile cilium / neuromuscular process controlling balance / stem cell division / nuclear migration / dynein complex binding / cell leading edge / transmission of nerve impulse / dynein intermediate chain binding / germ cell development / establishment of mitotic spindle orientation / dynactin binding / protein secretion / cochlea development / neuroblast proliferation / positive regulation of axon extension / microtubule-based process / phospholipase binding / lipid catabolic process / cytoplasmic microtubule / COPI-mediated anterograde transport / JNK cascade / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / cytoplasmic microtubule organization / axon cytoplasm / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / stress granule assembly / MHC class II antigen presentation / positive regulation of mitotic cell cycle / Recruitment of NuMA to mitotic centrosomes / regulation of microtubule cytoskeleton organization / Anchoring of the basal body to the plasma membrane / regulation of mitotic spindle organization / Resolution of Sister Chromatid Cohesion / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / adult locomotory behavior / AURKA Activation by TPX2 / mitotic spindle organization / hippocampus development / filopodium / phosphoprotein binding / RHO GTPases Activate Formins / modulation of chemical synaptic transmission / cerebral cortex development / kinetochore / Aggrephagy / microtubule cytoskeleton organization / Schaffer collateral - CA1 synapse / Separation of Sister Chromatids / neuron migration / HCMV Early Events / Regulation of PLK1 Activity at G2/M Transition / azurophil granule lumen

ドメイン・相同性:

: / : / PAC1 LisH domain / Dynein regulator LIS1 / LIS1, N-terminal / Lissencephaly type-1-like homology motif / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / LIS1 homology (LisH) motif profile. / LIS1 homology motif / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / : / Dynein heavy chain, ATPase lid domain / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / P-loop containing dynein motor region / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / WD domain, G-beta repeat / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase

構成要素:

Platelet-activating factor acetylhydrolase IB subunit beta / Cytoplasmic dynein 1 heavy chain 1

• 生物種: 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: 2.86 Å
• データ登録者: Yang J / Zhang K

資金援助

米国, 1件

Organization	Grant number	国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R35 GM142959	米国

• 引用: ジャーナル: Nat Chem Biol / 年: 2025; タイトル: Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1.; 著者: Jun Yang / Yuanchang Zhao / Pengxin Chai / Ahmet Yildiz / Kai Zhang / ; 要旨: Cytoplasmic dynein 1 (dynein) is the primary motor responsible for the retrograde transport of intracellular cargoes along microtubules. Activation of dynein requires the opening its autoinhibited Phi conformation, a process driven by Lis1 and Nde1/Ndel1. Using biochemical reconstitution and cryo-electron microscopy, we demonstrate that Nde1 enhances Lis1 binding to autoinhibited dynein and facilitates Phi opening. We identify a key intermediate in this activation pathway where a single Lis1 dimer binds between Phi-like (Phi) motor rings. In this 'Phi-Lis1' complex, Lis1 interacts with one motor domain through canonical sites at the AAA+ (adenosine triphosphatases associated with diverse cellular activities) ring and stalk, and with AAA5, AAA6 and linker regions of the other motor domain. Mutagenesis and motility assays confirm the critical role of the Phi-Lis1 interface in dynein activation. This intermediate forms rapidly in the presence of Nde1, although Nde1 is not part of Phi-Lis1. These findings provide key insights into how Nde1 promotes Lis1-mediated Phi opening.

履歴

登録	2024年10月21日	-
ヘッダ(付随情報) 公開	2025年8月6日	-
マップ公開	2025年8月6日	-
更新	2025年8月13日	-
現状	2025年8月13日	処理サイト: RCSB / 状態: 公開

マップ

• ファイル: ダウンロード / ファイル: emd_47378.map.gz / 形式: CCP4 / 大きさ: 216 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• 注釈: Sharpened map for for dimeric motor domains of phi-like dynein-1 bound to a Lis1 dimer under Nde1_Lis1 condition
• ボクセルのサイズ: X=Y=Z: 1.1573 Å

密度

表面レベル	登録者による: 0.3
最小 - 最大	-0.6985402 - 1.4977367
平均 (標準偏差)	-0.00008791265 (±0.043627422)

• 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 384 384 384 Spacing 384 384 384
セル	A=B=C: 444.4032 Å α=β=γ: 90.0 °

添付データ

マスク #1

• ファイル: emd_47378_msk_1.map

追加マップ: Unsharpened map for for dimeric motor domains of...

• ファイル: emd_47378_additional_1.map
• 注釈: Unsharpened map for for dimeric motor domains of phi-like dynein-1 bound to a Lis1 dimer under Nde1_Lis1 condition

ハーフマップ: Half map for for dimeric motor domains of...

• ファイル: emd_47378_half_map_1.map
• 注釈: Half map for for dimeric motor domains of phi-like dynein-1 bound to a Lis1 dimer under Nde1_Lis1 condition

ハーフマップ: Half map for for dimeric motor domains of...

• ファイル: emd_47378_half_map_2.map
• 注釈: Half map for for dimeric motor domains of phi-like dynein-1 bound to a Lis1 dimer under Nde1_Lis1 condition

試料の構成要素

全体 : Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dime...

• 全体: 名称: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Nde1-Lis1 condition

要素

• 複合体: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Nde1-Lis1 condition
  • タンパク質・ペプチド: Cytoplasmic dynein 1 heavy chain 1
  • タンパク質・ペプチド: Platelet-activating factor acetylhydrolase IB subunit beta
• リガンド: ADENOSINE-5'-DIPHOSPHATE
• リガンド: ADENOSINE-5'-TRIPHOSPHATE
• リガンド: MAGNESIUM ION

超分子 #1: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dime...

• 超分子: 名称: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Nde1-Lis1 condition; タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#2
• 由来(天然): 生物種: Homo sapiens (ヒト)
• 分子量: 理論値: 1.5 MDa

分子 #1: Cytoplasmic dynein 1 heavy chain 1

• 分子: 名称: Cytoplasmic dynein 1 heavy chain 1 / タイプ: protein_or_peptide / ID: 1 / コピー数: 2 / 光学異性体: LEVO
• 由来(天然): 生物種: Homo sapiens (ヒト)
• 分子量: 理論値: 533.08325 KDa
• 組換発現: 生物種: Spodoptera frugiperda (ツマジロクサヨトウ)

配列

文字列:

MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVG DEGEEEKEFI SYNINIDIHY GVKSNSLAFI KRTPVIDADK PVSSQLRVLT LSEDSPYETL HSFISNAVAP F FKSYIRES GKADRDGDKM APSVEKKIAE LEMGLLHLQQ NIEIPEISLP IHPMITNVAK QCYERGEKPK VTDFGDKVED PT FLNQLQS GVNRWIREIQ KVTKLDRDPA SGTALQEISF WLNLERALYR IQEKRESPEV LLTLDILKHG KRFHATVSFD TDT GLKQAL ETVNDYNPLM KDFPLNDLLS ATELDKIRQA LVAIFTHLRK IRNTKYPIQR ALRLVEAISR DLSSQLLKVL GTRK LMHVA YEEFEKVMVA CFEVFQTWDD EYEKLQVLLR DIVKRKREEN LKMVWRINPA HRKLQARLDQ MRKFRRQHEQ LRAVI VRVL RPQVTAVAQQ NQGEVPEPQD MKVAEVLFDA ADANAIEEVN LAYENVKEVD GLDVSKEGTE AWEAAMKRYD ERIDRV ETR ITARLRDQLG TAKNANEMFR IFSRFNALFV RPHIRGAIRE YQTQLIQRVK DDIESLHDKF KVQYPQSQAC KMSHVRD LP PVSGSIIWAK QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTI E STRVRGRTGN VLKLKVNFLP EIITLSKEVR NLKWLGFRVP LAIVNKAHQA NQLYPFAISL IESVRTYERT CEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLN LHSYSNLPIW VNKLDMEIER ILGVRLQAGL RAWTQVLLGQ AEDKAEVDMD TDAPQVSHKP GGEPKIKNVV H ELRITNQV IYLNPPIEEC RYKLYQEMFA WKMVVLSLPR IQSQRYQVGV HYELTEEEKF YRNALTRMPD GPVALEESYS AV MGIVSEV EQYVKVWLQY QCLWDMQAEN IYNRLGEDLN KWQALLVQIR KARGTFDNAE TKKEFGPVVI DYGKVQSKVN LKY DSWHKE VLSKFGQMLG SNMTEFHSQI SKSRQELEQH SVDTASTSDA VTFITYVQSL KRKIKQFEKQ VELYRNGQRL LEKQ RFQFP PSWLYIDNIE GEWGAFNDIM RRKDSAIQQQ VANLQMKIVQ EDRAVESRTT DLLTDWEKTK PVTGNLRPEE ALQAL TIYE GKFGRLKDDR EKCAKAKEAL ELTDTGLLSG SEERVQVALE ELQDLKGVWS ELSKVWEQID QMKEQPWVSV QPRKLR QNL DALLNQLKSF PARLRQYASY EFVQRLLKGY MKINMLVIEL KSEALKDRHW KQLMKRLHVN WVVSELTLGQ IWDVDLQ KN EAIVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN SVSAMKLSPY YKVFEEDA L SWEDKLNRIM ALFDVWIDVQ RRWVYLEGIF TGSADIKHLL PVETQRFQSI STEFLALMKK VSKSPLVMDV LNIQGVQRS LERLADLLGK IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILNEDN SVVLGISSRE GEEVMFKTP VSITEHPKIN EWLTLVEKEM RVTLAKLLAE SVTEVEIFGK ATSIDPNTYI TWIDKYQAQL VVLSAQIAWS E NVETALSS MGGGGDAAPL HSVLSNVEVT LNVLADSVLM EQPPLRRRKL EHLITELVHQ RDVTRSLIKS KIDNAKSFEW LS QMRFYFD PKQTDVLQQL SIQMANAKFN YGFEYLGVQD KLVQTPLTDR CYLTMTQALE ARLGGSPFGP AGTGKTESVK ALG HQLGRF VLVFNCDETF DFQAMGRIFV GLCQVGAWGC FDEFNRLEER MLSAVSQQVQ CIQEALREHS NPNYDKTSAP ITCE LLNKQ VKVSPDMAIF ITMNPGYAGR SNLPDNLKKL FRSLAMTKPD RQLIAQVMLY SQGFRTAEVL ANKIVPFFKL CDEQL SSQS HYDFGLRALK SVLVSAGNVK RERIQKIKRE KEERGEAVDE GEIAENLPEQ EILIQSVCET MVPKLVAEDI PLLFSL LSD VFPGVQYHRG EMTALREELK KVCQEMYLTY GDGEEVGGMW VEKVLQLYQI TQINHGLMMV GPSGSGKSMA WRVLLKA LE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDSVR GELQKRQWIV FDGDVDPEWV ENLNSVLD D NKLLTLPNGE RLSLPPNVRI MFEVQDLKYA TLATVSRCGM VWFSEDVLST DMIFNNFLAR LRSIPLDEGE DEAQRRRKG KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQIEQLERY IQRYLVYAIL WSLSGDSRLK MRAELGEYIR RITTVPLPTA PNIPIIDYEV SISGEWSPWQ AKVPQIEVET H KVAAPDVV VPTLDTVRHE ALLYTWLAEH KPLVLCGPPG SGKTMTLFSA LRALPDMEVV GLNFSSATTP ELLLKTFDHY CE YRRTPNG VVLAPVQLGK WLVLFCDEIN LPDMDKYGTQ RVISFIRQMV EHGGFYRTSD QTWVKLERIQ FVGACNPPTD PGR KPLSHR FLRHVPVVYV DYPGPASLTQ IYGTFNRAML RLIPSLRTYA EPLTAAMVEF YTMSQERFTQ DTQPHYIYSP REMT RWVRG IFEALRPLET LPVEGLIRIW AHEALRLFQD RLVEDEERRW TDENIDTVAL KHFPNIDREK AMSRPILYSN WLSKD YIPV DQEELRDYVK ARLKVFYEEE LDVPLVLFNE VLDHVLRIDR IFRQPQGHLL LIGVSGAGKT TLSRFVAWMN GLSVYQ IKV HRKYTGEDFD EDLRTVLRRS GCKNEKIAFI MDESNVLDSG FLERMNTLLA NGEVPGLFEG DEYATLMTQC KEGAQKE GL MLDSHEELYK WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNY I VPDYMPVVYD KLPQPPSHRE AIVNSCVFVH QTLHQANARL AKRGGRTMAI TPRHYLDFIN HYANLFHEKR SELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAV IEAQNAVKSI KKQHLVEVRS MANPPAAVKL ALESICLLLG ESTTDWKQIR SIIMRENFIP TIVNFSAEEI S DAIREKMK KNYMSNPSYN YEIVNRASLA CGPMVKWAIA QLNYADMLKR VEPLRNELQK LEDDAKDNQQ KANEVEQMIR DL EASIARY KEEYAVLISE AQAIKADLAA VEAKVNRSTA LLKSLSAERE RWEKTSETFK NQMSTIAGDC LLSAAFIAYA GYF DQQMRQ NLFTTWSHHL QQANIQFRTD IARTEYLSNA DERLRWQASS LPADDLCTEN AIMLKRFNRY PLIIDPSGQA TEFI MNEYK DRKITRTSFL DDAFRKNLES ALRFGNPLLV QDVESYDPVL NPVLNREVRR TGGRVLITLG DQDIDLSPSF VIFLS TRDP TVEFPPDLCS RVTFVNFTVT RSSLQSQCLN EVLKAERPDV DEKRSDLLKL QGEFQLRLRQ LEKSLLQALN EVKGRI LDD DTIITTLENL KREAAEVTRK VEETDIVMQE VETVSQQYLP LSTACSSIYF TMESLKQIHF LYQYSLQFFL DIYHNVL YE NPNLKGVTDH TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD AEFQHFLRGN EIVLSAGS T PRIQGLTVEQ AEAVVRLSCL PAFKDLIAKV QADEQFGIWL DSSSPEQTVP YLWSEETPAT PIGQAIHRLL LIQAFRPDR LLAMAHMFVS TNLGESFMSI MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVK SGRWVMLKNV HLAPGWLMQL EKKLHSLQPH ACFRLFLTME INPKVPVNLL RAGRIFVFEP PPGVKANMLR T FSSIPVSR ICKSPNERAR LYFLLAWFHA IIQERLRYAP LGWSKKYEFG ESDLRSACDT VDTWLDDTAK GRQNISPDKI PW SALKTLM AQSIYGGRVD NEFDQRLLNT FLERLFTTRS FDSEFKLACK VDGHKDIQMP DGIRREEFVQ WVELLPDTQT PSW LGLPNN AERVLLTTQG VDMISKMLKM QMLEDEDDLA YAETEKKTRT DSTSDGRPAW MRTLHTTASN WLHLIPQTLS HLKR TVENI KDPLFRFFER EVKMGAKLLQ DVRQDLADVV QVCEGKKKQT NYLRTLINEL VKGILPRSWS HYTVPAGMTV IQWVS DFSE RIKQLQNISL AAASGGAKEL KNIHVCLGGL FVPEAYITAT RQYVAQANSW SLEELCLEVN VTTSQGATLD ACSFGV TGL KLQGATCNNN KLSLSNAIST ALPLTQLRWV KQTNTEKKAS VVTLPVYLNF TRADLIFTVD FEIATKEDPR SFYERGV AV LCTE

UniProtKB: Cytoplasmic dynein 1 heavy chain 1

分子 #2: Platelet-activating factor acetylhydrolase IB subunit beta

• 分子: 名称: Platelet-activating factor acetylhydrolase IB subunit beta; タイプ: protein_or_peptide / ID: 2 / コピー数: 2 / 光学異性体: LEVO
• 由来(天然): 生物種: Homo sapiens (ヒト)
• 分子量: 理論値: 46.709984 KDa
• 組換発現: 生物種: Spodoptera frugiperda (ツマジロクサヨトウ)

配列

文字列:

MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL LEKKWTSVIR LQKKVMELES KLNEAKEEFT SGGPLGQKR DPKEWIPRPP EKYALSGHRS PVTRVIFHPV FSVMVSASED ATIKVWDYET GDFERTLKGH TDSVQDISFD H SGKLLASC SADMTIKLWD FQGFECIRTM HGHDHNVSSV AIMPNGDHIV SASRDKTIKM WEVQTGYCVK TFTGHREWVR MV RPNQDGT LIASCSNDQT VRVWVVATKE CKAELREHEH VVECISWAPE SSYSSISEAT GSETKKSGKP GPFLLSGSRD KTI KMWDVS TGMCLMTLVG HDNWVRGVLF HSGGKFILSC ADDKTLRVWD YKNKRCMKTL NAHEHFVTSL DFHKTAPYVV TGSV DQTVK VWECR

UniProtKB: Platelet-activating factor acetylhydrolase IB subunit beta

分子 #3: ADENOSINE-5'-DIPHOSPHATE

• 分子: 名称: ADENOSINE-5'-DIPHOSPHATE / タイプ: ligand / ID: 3 / コピー数: 6 / 式: ADP
• 分子量: 理論値: 427.201 Da

Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子*YM

分子 #4: ADENOSINE-5'-TRIPHOSPHATE

• 分子: 名称: ADENOSINE-5'-TRIPHOSPHATE / タイプ: ligand / ID: 4 / コピー数: 2 / 式: ATP
• 分子量: 理論値: 507.181 Da

Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子*YM

分子 #5: MAGNESIUM ION

• 分子: 名称: MAGNESIUM ION / タイプ: ligand / ID: 5 / コピー数: 4 / 式: MG
• 分子量: 理論値: 24.305 Da

実験情報

構造解析

• 手法: クライオ電子顕微鏡法
• 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: 7.2 ; 詳細: 25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 3 mM ATP
• 凍結: 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 278 K / 装置: FEI VITROBOT MARK IV

電子顕微鏡法

• 顕微鏡: TFS GLACIOS
• 撮影: フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均電子線量: 40.0 e/Ų
• 電子線: 加速電圧: 200 kV / 電子線源: FIELD EMISSION GUN
• 電子光学系: C2レンズ絞り径: 30.0 µm / 最大 デフォーカス（補正後）: 3.0 µm / 最小 デフォーカス（補正後）: 1.2 µm / 倍率（補正後）: 45000 / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 最大 デフォーカス（公称値）: 3.0 µm / 最小 デフォーカス（公称値）: 1.2 µm / 倍率（公称値）: 45000
• 試料ステージ: 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER; ホルダー冷却材: NITROGEN

画像解析

• CTF補正: タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION
• 初期モデル: モデルのタイプ: NONE
• 最終 再構成: 解像度のタイプ: BY AUTHOR / 解像度: 2.86 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 215049
• 初期 角度割当: タイプ: MAXIMUM LIKELIHOOD
• 最終 角度割当: タイプ: MAXIMUM LIKELIHOOD