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データを開く
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基本情報
登録情報 | ![]() | |||||||||
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タイトル | Maps of Collagen VI half- and full-beads | |||||||||
![]() | full-bead map, with one of the half-beads not in focus | |||||||||
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![]() | Collagen / Extracellular matrix / STRUCTURAL PROTEIN | |||||||||
機能・相同性 | ![]() response to polyamine macromolecule / response to bleomycin / regulation of collagen fibril organization / muscle cell apoptotic process / collagen type VI trimer / multicellular organismal locomotion / muscle system process / apoptotic nuclear changes / caveola assembly / reduction of food intake in response to dietary excess ...response to polyamine macromolecule / response to bleomycin / regulation of collagen fibril organization / muscle cell apoptotic process / collagen type VI trimer / multicellular organismal locomotion / muscle system process / apoptotic nuclear changes / caveola assembly / reduction of food intake in response to dietary excess / limb joint morphogenesis / mitochondrial transmembrane transport / skeletal muscle tissue growth / fat cell proliferation / extracellular matrix assembly / Collagen chain trimerization / response to decreased oxygen levels / extracellular matrix structural constituent conferring tensile strength / platelet-derived growth factor binding / response to peptide / tissue remodeling / skeletal muscle fiber differentiation / basement membrane organization / lung epithelial cell differentiation / Collagen biosynthesis and modifying enzymes / sensory perception of mechanical stimulus / collagen metabolic process / Signaling by PDGF / mitochondrial depolarization / myelination in peripheral nervous system / 2-oxoglutarate metabolic process / respiratory system process / energy reserve metabolic process / collagen trimer / skeletal muscle tissue regeneration / NCAM1 interactions / collagen fibril organization / cartilage development / Assembly of collagen fibrils and other multimeric structures / response to pain / muscle organ development / response to muscle activity / regulation of cell size / lung alveolus development / intracellular vesicle / bone mineralization / transmission of nerve impulse / endodermal cell differentiation / myofibril / uterus development / lung morphogenesis / Collagen degradation / basement membrane / homeostasis of number of cells / single fertilization / hair follicle development / ECM proteoglycans / Integrin cell surface interactions / canonical Wnt signaling pathway / adipose tissue development / response to glucose / response to UV / response to mechanical stimulus / skeletal muscle fiber development / collagen binding / tricarboxylic acid cycle / extracellular matrix / reactive oxygen species metabolic process / insulin-like growth factor receptor signaling pathway / sarcoplasmic reticulum / response to reactive oxygen species / glycolytic process / mitochondrion organization / phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein tetramerization / cellular response to amino acid stimulus / serine-type endopeptidase inhibitor activity / cell morphogenesis / sarcolemma / bone development / autophagy / response to wounding / response to toxic substance / circadian rhythm / osteoblast differentiation / insulin receptor signaling pathway / extracellular vesicle / heart development / : / neuron apoptotic process / gene expression / response to lipopolysaccharide / cell adhesion / inflammatory response / endoplasmic reticulum lumen / response to xenobiotic stimulus / lysosomal membrane / protein-containing complex / mitochondrion / extracellular space 類似検索 - 分子機能 | |||||||||
生物種 | ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 15.0 Å | |||||||||
![]() | Schulte T / Speranzini V / Chaves-Sanjuan A / Ricagno S | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Helical superstructures between amyloid and collagen in cardiac fibrils from a patient with AL amyloidosis. 著者: Tim Schulte / Antonio Chaves-Sanjuan / Valentina Speranzini / Kevin Sicking / Melissa Milazzo / Giulia Mazzini / Paola Rognoni / Serena Caminito / Paolo Milani / Chiara Marabelli / Alessandro ...著者: Tim Schulte / Antonio Chaves-Sanjuan / Valentina Speranzini / Kevin Sicking / Melissa Milazzo / Giulia Mazzini / Paola Rognoni / Serena Caminito / Paolo Milani / Chiara Marabelli / Alessandro Corbelli / Luisa Diomede / Fabio Fiordaliso / Luigi Anastasia / Carlo Pappone / Giampaolo Merlini / Martino Bolognesi / Mario Nuvolone / Rubén Fernández-Busnadiego / Giovanni Palladini / Stefano Ricagno / ![]() ![]() ![]() ![]() 要旨: Systemic light chain (LC) amyloidosis (AL) is a disease where organs are damaged by an overload of a misfolded patient-specific antibody-derived LC, secreted by an abnormal B cell clone. The high LC ...Systemic light chain (LC) amyloidosis (AL) is a disease where organs are damaged by an overload of a misfolded patient-specific antibody-derived LC, secreted by an abnormal B cell clone. The high LC concentration in the blood leads to amyloid deposition at organ sites. Indeed, cryogenic electron microscopy (cryo-EM) has revealed unique amyloid folds for heart-derived fibrils taken from different patients. Here, we present the cryo-EM structure of heart-derived AL amyloid (AL59) from another patient with severe cardiac involvement. The double-layered structure displays a u-shaped core that is closed by a β-arc lid and extended by a straight tail. Noteworthy, the fibril harbours an extended constant domain fragment, thus ruling out the variable domain as sole amyloid building block. Surprisingly, the fibrils were abundantly concatenated with a proteinaceous polymer, here identified as collagen VI (COLVI) by immuno-electron microscopy (IEM) and mass-spectrometry. Cryogenic electron tomography (cryo-ET) showed how COLVI wraps around the amyloid forming a helical superstructure, likely stabilizing and protecting the fibrils from clearance. Thus, here we report structural evidence of interactions between amyloid and collagen, potentially signifying a distinct pathophysiological mechanism of amyloid deposits. | |||||||||
履歴 |
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構造の表示
添付画像 |
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ダウンロードとリンク
-EMDBアーカイブ
マップデータ | ![]() | 203.8 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 28.5 KB 28.5 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 13 KB | 表示 | ![]() |
画像 | ![]() | 33 KB | ||
マスクデータ | ![]() | 216 MB | ![]() | |
Filedesc metadata | ![]() | 8.8 KB | ||
その他 | ![]() ![]() ![]() ![]() | 111.9 MB 113.8 MB 200.6 MB 200.6 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||
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注釈 | full-bead map, with one of the half-beads not in focus | ||||||||||||||||||||||||||||||||||||
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: 2.607 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-マスク #1
ファイル | ![]() | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-追加マップ: #1
ファイル | emd_18689_additional_1.map | ||||||||||||
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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 obtained by fitting the focused half-bead...
ファイル | emd_18689_additional_2.map | ||||||||||||
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注釈 | composite map obtained by fitting the focused half-bead map into the unfocused half-bead of the full map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: half-map A associated with main map
ファイル | emd_18689_half_map_1.map | ||||||||||||
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注釈 | half-map A associated with main map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: half-map B associated with main map
ファイル | emd_18689_half_map_2.map | ||||||||||||
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注釈 | half-map B associated with main map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
-全体 : Collagen VI bead
全体 | 名称: Collagen VI bead |
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要素 |
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-超分子 #1: Collagen VI bead
超分子 | 名称: Collagen VI bead / タイプ: organelle_or_cellular_component / ID: 1 / 親要素: 0 / 含まれる分子: all 詳細: Collagen VI co-extracted with light chain amyloid AL59 |
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由来(天然) | 生物種: ![]() |
-分子 #1: CO6A1_HUMAN; Collagen alpha-1(VI) chain
分子 | 名称: CO6A1_HUMAN; Collagen alpha-1(VI) chain / タイプ: protein_or_peptide / ID: 1 / 詳細: CO6A1_HUMAN; Collagen alpha-1(VI) chain; P12109 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
配列 | 文字列: MRAARALLPL LLQACWTAAQ DEPETPRAVA FQDCPVDLFF VLDTSESVAL RLKPYGALVD KVKSFTKRFI DNLRDRYYRC DRNLVWNAGA LHYSDEVEII QGLTRMPGGR DALKSSVDAV KYFGKGTYTD CAIKKGLEQL LVGGSHLKEN KYLIVVTDGH PLEGYKEPCG ...文字列: MRAARALLPL LLQACWTAAQ DEPETPRAVA FQDCPVDLFF VLDTSESVAL RLKPYGALVD KVKSFTKRFI DNLRDRYYRC DRNLVWNAGA LHYSDEVEII QGLTRMPGGR DALKSSVDAV KYFGKGTYTD CAIKKGLEQL LVGGSHLKEN KYLIVVTDGH PLEGYKEPCG GLEDAVNEAK HLGVKVFSVA ITPDHLEPRL SIIATDHTYR RNFTAADWGQ SRDAEEAISQ TIDTIVDMIK NNVEQVCCSF ECQPARGPPG LRGDPGFEGE RGKPGLPGEK GEAGDPGRPG DLGPVGYQGM KGEKGSRGE KGSRGPKGYK GEKGKRGIDG VDGVKGEMGY PGLPGCKGSP GFDGIQGPPG PKGDPGAFGL KGEKGEPGAD GEAGRPGSSG PSGDEGQPGE PGPPGEKGEA GDEGNPGPDG APGERGGPGE RGPRGTPGTR GPRGDPGEAG PQGDQGREGP VGVPGDPGEA GPIGPKGYRG DEGPPGSEGA RGAPGPAGPP GDPGLMGERG EDGPAGNGTE GFPGFPGYPG NRGAPGINGT KGYPGLKGDE GEAGDPGDDN NDIAPRGVKG AKGYRGPEGP QGPPGHQGPP GPDECEILDI IMKMCSCCEC KCGPIDLLFV LDSSESIGLQ NFEIAKDFVV KVIDRLSRDE LVKFEPGQSY AGVVQYSHSQ MQEHVSLRSP SIRNVQELKE AIKSLQWMAG GTFTGEALQY TRDQLLPPSP NNRIALVITD GRSDTQRDTT PLNVLCSPGI QVVSVGIKDV FDFIPGSDQL NVISCQGLAP SQGRPGLSLV KENYAELLED AFLKNVTAQI CIDKKCPDYT CPITFSSPAD ITILLDGSAS VGSHNFDTTK RFAKRLAERF LTAGRTDPAH DVRVAVVQYS GTGQQRPERA SLQFLQNYTA LASAVDAMDF INDATDVNDA LGYVTRFYRE ASSGAAKKRL LLFSDGNSQG ATPAAIEKAV Q EAQRAGIE IFVVVVGRQV NEPHIRVLVT GKTAEYDVAY GESHLFRVPS YQALLRGVFH QTVSRKVALG UniProtKB: Collagen alpha-1(VI) chain |
-分子 #2: CO6A2_HUMAN; Collagen alpha-2(VI) chain
分子 | 名称: CO6A2_HUMAN; Collagen alpha-2(VI) chain / タイプ: protein_or_peptide / ID: 2 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
配列 | 文字列: MLQGTCSVLL LWGILGAIQA QQQEVISPDT TERNNNCPEK TDCPIHVYFV LDTSESVTMQ SPTDILLFHM KQFVPQFISQ LQNEFYLDQV ALSWRYGGLH FSDQVEVFSP PGSDRASFIK NLQGISSFRR GTFTDCALAN MTEQIRQDRS KGTVHFAVVI TDGHVTGSPC ...文字列: MLQGTCSVLL LWGILGAIQA QQQEVISPDT TERNNNCPEK TDCPIHVYFV LDTSESVTMQ SPTDILLFHM KQFVPQFISQ LQNEFYLDQV ALSWRYGGLH FSDQVEVFSP PGSDRASFIK NLQGISSFRR GTFTDCALAN MTEQIRQDRS KGTVHFAVVI TDGHVTGSPC GGIKLQAERA REEGIRLFAV APNQNLKEQG LRDIASTPHE LYRNDYATML PDSTEIDQDT INRIIKVMKH EAYGECYKVS CLEIPGPSGP KGYRGQKGAK GNMGEPGEPG QKGRQGDPGI EGPIGFPGPK GVPGFKGEKG EFGADGRKGA PGLAGKNGTD GQKGKLGRIG PPGCKGDPGN RGPDGYPGEA GSPGERGDQG GKGDPGRPGR RGPPGEIGAK GSKGYQGNSG APGSPGVKGA KGGPGPRGPK GEPGRRGDPG TKGSPGSDGP KGEKGDPGPE GPRGLAGEVG NKGAKGDRGL PGPRGPQGAL GEPGKQGSRG DPGDAGPRGD SGQPGPKGDP GRPGFSYPGP RGAPGEKGEP GPRGPEGGRG DFGLKGEPGR KGEKGEPADP GPPGEPGPRG PRGVPGPEGE PGPPGDPGLT ECDVMTYVRE TCGCCDCEKR CGALDVVFVI DSSESIGYTN FTLEKNFVIN VVNRLGAIAK DPKSETGTRV GVVQYSHEGT FEAIQLDDER IDSLSSFKEA VKNLEWIAGG TWTPSALKFA YDRLIKESRR QKTRVFAVVI TDGRHDPRDD DLNLRALCDR DVTVTAIGIG DMFHEKHESE NLYSIACDKP QQVRNMTLFS DLVAEKFIDD MEDVLCPDPQ IVCPDLPCQT ELSVAQCTQR PVDIVFLLDG SERLGEQNFH KARRFVEQVA RRLTLARRDD DPLNARVALL QFGGPGEQQV AFPLSHNLTA IHEALETTQY LNSFSHVGAG VVHAINAIVR SPRGGARRHA ELSFVFLTDG VTGNDSLHES AHSMRKQNVV PTVLALGSDV DMDVLTTLSL GDRAAVFHEK DYDSLAQPGF FDRFIRWIC UniProtKB: Collagen alpha-2(VI) chain |
-分子 #3: CO6A3_HUMAN; Collagen alpha-3(VI) chain
分子 | 名称: CO6A3_HUMAN; Collagen alpha-3(VI) chain / タイプ: protein_or_peptide / ID: 3 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
配列 | 文字列: MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI GEEHFQLVRE FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ EVLSHISNMS YIGGTNQTGK GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT DGHSKDGLAL PSAELKSADV ...文字列: MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI GEEHFQLVRE FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ EVLSHISNMS YIGGTNQTGK GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT DGHSKDGLAL PSAELKSADV NVFAIGVEDA DEGALKEIAS EPLNMHMFNL ENFTSLHDIV GNLVSCVHSS VSPERAGDTE TLKDITAQDS ADIIFLIDGS NNTGSVNFAV ILDFLVNLLE KLPIGTQQIR VGVVQFSDEP RTMFSLDTYS TKAQVLGAVK ALGFAGGELA NIGLALDFVV ENHFTRAGGS RVEEGVPQVL VLISAGPSSD EIRYGVVALK QASVFSFGLG AQAASRAELQ HIATDDNLVF TVPEFRSFGD LQEKLLPYIV GVAQRHIVLK PPTIVTQVIE VNKRDIVFLV DGSSALGLAN FNAIRDFIAK VIQRLEIGQD LIQVAVAQYA DTVRPEFYFN THPTKREVIT AVRKMKPLDG SALYTGSALD FVRNNLFTSS AGYRAAEGIP KLLVLITGGK SLDEISQPAQ ELKRSSIMAF AIGNKGADQA ELEEIAFDSS LVFIPAEFRA APLQGMLPGL LAPLRTLSGT PEVHSNKRDI IFLLDGSANV GKTNFPYVRD FVMNLVNSLD IGNDNIRVGL VQFSDTPVTE FSLNTYQTKS DILGHLRQLQ LQGGSGLNTG SALSYVYANH FTEAGGSRIR EHVPQLLLLL TAGQSEDSYL QAANALTRAG ILTFCVGASQ ANKAELEQIA FNPSLVYLMD DFSSLPALPQ QLIQPLTTYV SGGVEEVPLA QPESKRDILF LFDGSANLVG QFPVVRDFLY KIIDELNVKP EGTRIAVAQY SDDVKVESRF DEHQSKPEIL NLVKRMKIKT GKALNLGYAL DYAQRYIFVK SAGSRIEDGV LQFLVLLVAG RSSDRVDGPA SNLKQSGVVP FIFQAKNADP AELEQIVLSP AFILAAESLP KIGDLHPQIV NLLKSVHNGA PAPVSGEKDV VFLLDGSEGV RSGFPLLKEF VQRVVESLDV GQDRVRVAVV QYSDRTRPEF YLNSYMNKQD VVNAVRQLTL LGGPTPNTGA ALEFVLRNIL VSSAGSRITE GVPQLLIVLT ADRSGDDVRN PSVVVKRGGA VPIGIGIGNA DITEMQTISF IPDFAVAIPT FRQLGTVQQV ISERVTQLTR EELSRLQPVL QPLPSPGVGG KRDVVFLIDG SQSAGPEFQY VRTLIERLVD YLDVGFDTTR VAVIQFSDDP KVEFLLNAHS SKDEVQNAVQ RLRPKGGRQI NVGNALEYVS RNIFKRPLGS RIEEGVPQFL VLISSGKSDD EVDDPAVELK QFGVAPFTIA RNADQEELVK ISLSPEYVFS VSTFRELPSL EQKLLTPITT LTSEQIQKLL ASTRYPPPAV ESDAADIVFL IDSSEGVRPD GFAHIRDFVS RIVRRLNIGP SKVRVGVVQF SNDVFPEFYL KTYRSQAPVL DAIRRLRLRG GSPLNTGKAL EFVARNLFVK SAGSRIEDGV PQHLVLVLGG KSQDDVSRFA QVIRSSGIVS LGVGDRNIDR TELQTITNDP RLVFTVREFR ELPNIEERIM NSFGPSAATP APPGVDTPPP SRPEKKKADI VFLLDGSINF RRDSFQEVLR FVSEIVDTVY EDGDSIQVGL VQYNSDPTDE FFLKDFSTKR QIIDAINKVV YKGGRHANTK VGLEHLRVNH FVPEAGSRLD QRVPQIAFVI TGGKSVEDAQ DVSLALTQRG VKVFAVGVRN IDSEEVGKIA SNSATAFRVG NVQELSELSE QVLETLHDAM HETLCPGVTD AAKACNLDVI LGFDGSRDQN VFVAQKGFES KVDAILNRIS QMHRVSCSGG RSPTVRVSVV ANTPSGPVEA FDFDEYQPEM LEKFRNMRSQ HPYVLTEDTL KVYLNKFRQS SPDSVKVVIH FTDGADGDLA DLHRASENLR QEGVRALILV GLERVVNLER LMHLEFGRGF MYDRPLRLNL LDLDYELAEQ LDNIAEKACC GVPCKCSGQR GDRGPIGSIG PKGIPGEDGY RGYPGDEGGP GERGPPGVNG TQGFQGCPGQ RGVKGSRGFP GEKGEVGEIG LDGLDGEDGD KGLPGSSGEK GNPGRRGDKG PRGEKGERGD VGIRGDPGNP GQDSQERGPK GETGDLGPMG VPGRDGVPGG PGETGKNGGF GRRGPPGAKG NKGGPGQPGF EGEQGTRGAQ GPAGPAGPPG LIGEQGISGP RGSGGAAGAP GERGRTGPLG RKGEPGEPGP KGGIGNRGPR GETGDDGRDG VGSEGRRGKK GERGFPGYPG PKGNPGEPGL NGTTGPKGIR GRRGNSGPPG IVGQKGDPGY PGPAGPKGNR GDSIDQCALI QSIKDKCPCC YGPLECPVFP TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY NNEVTTEIRF ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK RVRNGFLMRK VAVFFSNTPT RASPQLREAV LKLSDAGITP LFLTRQEDRQ LINALQINNT AVGHALVLPA GRDLTDFLEN VLTCHVCLDI CNIDPSCGFG SWRPSFRDRR AAGSDVDIDM AFILDSAETT TLFQFNEMKK YIAYLVRQLD MSPDPKASQH FARVAVVQHA PSESVDNASM PPVKVEFSLT DYGSKEKLVD FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGEVPEQ QLEEAQRVIL QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK STELNEEPLM RFGRLLPSFV SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT KPVTTTTKPV TTTTKPVTII NQPSVKPAAA KPAPAKPVAA KPVATKMATV RPPVAVKPAT AAKPVAAKPA AVRPPAAAAA KPVATKPEVP RPQAAKPAAT KPATTKPMVK MSREVQVFEI TENSAKLHWE RAEPPGPYFY DLTVTSAHDQ SLVLKQNLTV TDRVIGGLLA GQTYHVAVVC YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS TEPLALTETD ICKLPKDEGT CRDFILKWYY DPNTKSCARF WYGGCGGNEN KFGSQKECEK VCAPVLAKPG VISVMGT UniProtKB: Collagen alpha-3(VI) chain |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7 |
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凍結 | 凍結剤: ETHANE / 装置: FEI VITROBOT MARK IV |
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電子顕微鏡法 #1
Microscopy ID | 1 |
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顕微鏡 | FEI TALOS ARCTICA |
撮影 | Image recording ID: 1 フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 検出モード: COUNTING / 実像数: 2049 / 平均電子線量: 40.0 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: ![]() |
電子光学系 | 倍率(補正後): 120000 / 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): 2.0 µm / 最小 デフォーカス(公称値): 0.5 µm |
試料ステージ | ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Talos Arctica / 画像提供: FEI Company |
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電子顕微鏡法 #1~
Microscopy ID | 1 |
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顕微鏡 | FEI TALOS ARCTICA |
撮影 | Image recording ID: 2 フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 検出モード: COUNTING / 実像数: 2556 / 平均電子線量: 40.0 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: ![]() |
電子光学系 | 倍率(補正後): 73000 / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 0.5 µm |
実験機器 | ![]() モデル: Talos Arctica / 画像提供: FEI Company |