[English] 日本語

- EMDB-52728: Spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ri... -
+
Open data
-
Basic information
Entry | ![]() | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis | ||||||||||||||||||||||||
![]() | Local resolution-filtered map after focused refinement of spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis | ||||||||||||||||||||||||
![]() |
| ||||||||||||||||||||||||
![]() | cytoskeleton / microtubule / microtubule nucleation / complex / template / cap / gamma-tubulin / gamma-tubulin ring complex / cell cycle / nedd1 / neural precursor cell-expressed developmentally down-regulated 1 | ||||||||||||||||||||||||
Function / homology | ![]() microtubule minus-end binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / interphase microtubule organizing center / gamma-tubulin complex / gamma-tubulin ring complex / microtubule nucleation / gamma-tubulin binding / mitotic spindle assembly / spindle assembly ...microtubule minus-end binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / interphase microtubule organizing center / gamma-tubulin complex / gamma-tubulin ring complex / microtubule nucleation / gamma-tubulin binding / mitotic spindle assembly / spindle assembly / cytoplasmic microtubule organization / meiotic cell cycle / spindle / spindle pole / mitotic cell cycle / microtubule / centrosome / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.5 Å | ||||||||||||||||||||||||
![]() | Vermeulen BJA / Pfeffer S | ||||||||||||||||||||||||
Funding support | ![]()
| ||||||||||||||||||||||||
![]() | ![]() Title: Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC. Authors: Qi Gao / Florian W Hofer / Sebastian Filbeck / Bram J A Vermeulen / Martin Würtz / Annett Neuner / Charlotte Kaplan / Maja Zezlina / Cornelia Sala / Hyesu Shin / Oliver J Gruss / Elmar ...Authors: Qi Gao / Florian W Hofer / Sebastian Filbeck / Bram J A Vermeulen / Martin Würtz / Annett Neuner / Charlotte Kaplan / Maja Zezlina / Cornelia Sala / Hyesu Shin / Oliver J Gruss / Elmar Schiebel / Stefan Pfeffer / ![]() Abstract: The γ-tubulin ring complex (γ-TuRC) acts as a structural template for microtubule formation at centrosomes, associating with two main compartments: the pericentriolar material and the centriole ...The γ-tubulin ring complex (γ-TuRC) acts as a structural template for microtubule formation at centrosomes, associating with two main compartments: the pericentriolar material and the centriole lumen. In the pericentriolar material, the γ-TuRC is involved in microtubule organization, while the function of the centriole lumenal pool remains unclear. The conformational landscape of the γ-TuRC, which is crucial for its activity, and its centrosomal anchoring mechanisms, which determine γ-TuRC activity and turnover, are not understood. Using cryo-electron tomography, we analyze γ-TuRCs in human cells and purified centrosomes. Pericentriolar γ-TuRCs simultaneously associate with the essential adapter NEDD1 and the microcephaly protein CDK5RAP2. NEDD1 forms a tetrameric structure at the γ-TuRC base through interactions with four GCP3/MZT1 modules and GCP5/6-specific extensions, while multiple copies of CDK5RAP2 engage the γ-TuRC in two distinct binding patterns to promote γ-TuRC closure and activation. In the centriole lumen, the microtubule branching factor Augmin tethers a condensed cluster of γ-TuRCs to the centriole wall with defined directional orientation. Centriole-lumenal γ-TuRC-Augmin is protected from degradation during interphase and released in mitosis to aid chromosome alignment. This study provides a unique view on γ-TuRC structure and molecular organization at centrosomes and identifies an important cellular function of centriole-lumenal γ-TuRCs. | ||||||||||||||||||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 198.7 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 23.6 KB 23.6 KB | Display Display | ![]() |
Images | ![]() | 90.7 KB | ||
Filedesc metadata | ![]() | 8.3 KB | ||
Others | ![]() ![]() | 172 MB 171.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9i8gC ![]() 9i8hC ![]() 9i8mC ![]() 9i8nC C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Local resolution-filtered map after focused refinement of spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.4267 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: Half map 2 for the focused refinement of...
File | emd_52728_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half map 2 for the focused refinement of spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Half map 1 for the focused refinement of...
File | emd_52728_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half map 1 for the focused refinement of spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : Tetramer of NEDD1 bound to the gamma-tubulin ring complex
Entire | Name: Tetramer of NEDD1 bound to the gamma-tubulin ring complex |
---|---|
Components |
|
-Supramolecule #1: Tetramer of NEDD1 bound to the gamma-tubulin ring complex
Supramolecule | Name: Tetramer of NEDD1 bound to the gamma-tubulin ring complex type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() |
-Macromolecule #1: Gamma-tubulin complex component 2
Macromolecule | Name: Gamma-tubulin complex component 2 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: MSEFRIHHDV NELISLLHVF GLEGADVYID LLQKNRTPYV TTSVSTHSAK VKIAEFSRTP DDFLKKYEE LKSKNTRNLD PLVYLLSKLI EDKETLQYLQ QNAKDKAELA TSSVTSVSLP I APNTSKIS MQELEELRRQ LETATVAVSC SHQPVEVLRK FLRDKLNKKH ...String: MSEFRIHHDV NELISLLHVF GLEGADVYID LLQKNRTPYV TTSVSTHSAK VKIAEFSRTP DDFLKKYEE LKSKNTRNLD PLVYLLSKLI EDKETLQYLQ QNAKDKAELA TSSVTSVSLP I APNTSKIS MQELEELRRQ LETATVAVSC SHQPVEVLRK FLRDKLNKKH TGHPVPVFPS WV YERPALT GDFMSFSNPS TDVTVSIGTL PLPSQETCLV EDLLYILIGV DGRYISVQPL VGR QSRSFS VEQNLDSSVK ELVNRILPVA TNYSTVTRFV EENSSFEYGQ VNHALGAAMR TLGK EYMIL ISQLEHLQRQ GLLSLQKLWF YIQPTLRTME VLASIATSLN KGECFGGATL SLLHD RTFG YTGDSQAQEL CLYLTKAASA PYFDILERWI YRGIINDPYS EFMVEEHELQ KEKIQE DYN DKYWDQRYTI VQQQIPSFLQ KVADKILSTG KYLNVVRECG HDVTCPDAKE ITYTLKE QA YVERIEKAYN YASKVLLDFL MEEEELVAHL RSIKHYFLMD QGDFFVHFMD LTEEELKK P VDDIIPTRLE ALLELALRMS TANTDPFKDD LKIELMPHDL ITQLLRVLAI ETHQEKALI NSDPTELALS GLESFSFDYI VKWPLSLIIN RKALTRYQML FRHMFYCKHV ERLLCNVWIS NKTAKQFSL HSAKWFAGAF TLRQRMLNFV QNIQYYMMFE VMEPTWHILE KNLKSASNID D VLSHHTSF LDNCLKDCML TNPELLKIFS KLMSVCVMFT NCLQRFTQSM QVQTEMEHLT LE HGTMMGP PTQCERTEEA LKKKLTSKYL EEHIDKFPSS FGFESTINNF DSNFSAHLMD LLD KLSMYS TSDCEHSMIN IIYRLDFNGF YTERLKQLSS ERNQKSAPLL GPAQHAVSTK UniProtKB: Gamma-tubulin complex component |
-Macromolecule #2: Gamma-tubulin complex component 3
Macromolecule | Name: Gamma-tubulin complex component 3 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: MAVPDQKSPN VLLQNLCCRI LGKGEADVAQ QFQYAVRVIG SNFAPTVERD EFLVTEKIKK EFVRQRREA DGALFSELHR KLQSQGVLKN RWSILYLLLS LSEDPRKQPN KTSSFAALFA Q ALPRDAHS TPYYYARPQS LPLSYQDRNV QCAQNAASIG SSGISSIGMY ...String: MAVPDQKSPN VLLQNLCCRI LGKGEADVAQ QFQYAVRVIG SNFAPTVERD EFLVTEKIKK EFVRQRREA DGALFSELHR KLQSQGVLKN RWSILYLLLS LSEDPRKQPN KTSSFAALFA Q ALPRDAHS TPYYYARPQS LPLSYQDRNV QCAQNAASIG SSGISSIGMY ALNGPTPQSI IQ GQSNQTP NMGDALRQQL GSRLAWTLAA GQQPSQQSTT TKGLPNTVSR NVPRTRREGD SSG SVEITE TSLVRDLLYV FQGIDGKFVK MCNSENCYKV DGKVAVSKSL KDITSKLSEL GWLH NKIKK YTDQRSLDRA FGLVGQSFCA ALHQELKEYY RLLSVLHSQL QVEDDQGVNL GVESS LTLR RLLVWTFDPK IRLKTLAALV DHCQGRKGGE LASAVHAYTK TGDPYMRSLV QHILGL VAY PILNFLYRWI YDGELEDTYH EFFVASDPVV KTDRLWHDKY SLRKSMIPSF MTMDQSR KV LLIGKSINFL HQVCHDQTPA SKAMAVGKSA ESPKDAAELF TDLENAFQTK IDAAYFDT S KYLLDVLNKN YNLLEHMQAM RRYLLLGQGD FIRHLMDLLK PELVRPATTL YQHNLTGIL ETAVRATNAQ FDNPEILKRL DVRLLEVSPG DTGWDVFSLD YHVDGPIATV FTRECMSHYL RVFNFLWRA KRMEYILTDI WKGHMCNAKL LKGMPELSGV LHQCHILASE MVHFIHQMQY Y ITFEVLEC SWDELWNKVL KAQDLDHIIA AHDVFLDTII SRCLLDSESR ALLNQLRAVF DQ IIEFQNA QDALYRAALE ELQQRLQFEE RKKERESEGE WGVTAAEEDV ENKRIQEFQE SIP KMRSQL RILTHFYQGI VQQFLVLLTT STDESLRFLS FRLDFNEHYK AREPRLRVSM GTRG RRSFH V UniProtKB: Gamma-tubulin complex component 3 homolog |
-Macromolecule #3: Gamma-tubulin complex component 4
Macromolecule | Name: Gamma-tubulin complex component 4 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: MIHELLLALS GYPGSIFTWN KRTGLQVSQD IPFLHPGETS VLNRLCKLGT DYIRFTEFIE QYTGHVQQQ DHHPSQQGQV GLHGIYLRAF CRGLDSILQP YRQALLDLEQ EFLADPHLSI S HINYSLDQ FHLLFPSIMV VVEQIKSQKI HGCQILETVY KHSCGGLPPV ...String: MIHELLLALS GYPGSIFTWN KRTGLQVSQD IPFLHPGETS VLNRLCKLGT DYIRFTEFIE QYTGHVQQQ DHHPSQQGQV GLHGIYLRAF CRGLDSILQP YRQALLDLEQ EFLADPHLSI S HINYSLDQ FHLLFPSIMV VVEQIKSQKI HGCQILETVY KHSCGGLPPV RSALEKTLAV CH GVMYKQL SAWMLHGLLL DQYEEFFVRQ GSSSGNLAAA FEEEEDDLGI GGLTGKQLRE LQD LRLIEE ENMLAPSLKQ FSLRAEMLPS YIPVRVAEKI LFVGESVQMF ENQNVNMSRT GSIL KNQED TFAAELHRLK QQPLFSLVDF ESVLDRIRST VAEHLWKLMV EESDLLGQLK IIKDF YLLG RGELFQAFID VAQNMLKTPP TAVTEHDVNV AFQLSAHKVL LDDDNLLPLL NLTIDY HGK EHKDTSQPRE GPFRDMSPRE APTSGWAALG LSYKVQWPLH ILFTPAVLEK YNVVFKY LL SVRRVQSELQ HCWALQMQRK HLESNKTDAI KWRLQNHMAF LVDNLQYYLQ VDVLESQF S QLLQQINSTR DFESIRLAHD HFLSNLLAQS FILLKPVFHC LNEILELCHS FCSLVSQNL GPLDERGAGQ LDILVKGFSC QSSLLFRILS SVRNHQINPD LAQLLLRLDY NKYYTQAGGT LGSFGL UniProtKB: Gamma-tubulin complex component |
-Macromolecule #4: Gamma-tubulin complex component 6
Macromolecule | Name: Gamma-tubulin complex component 6 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: MDSITKLFGD LCESHMVGFP WRTALNSRKH SKNRTKQTLK KLAYDTLFVH LFQDEARKLQ PNCTRLPVK NKIIMLSFNL RICGMSSEAD RLEELVEYLE QSNGIQISDL HAVLELLVEL S GTGPPQLL PPKRDYFKNN KYVGRNVKYQ GYDYYDVQVF EADLGTTVAY ...String: MDSITKLFGD LCESHMVGFP WRTALNSRKH SKNRTKQTLK KLAYDTLFVH LFQDEARKLQ PNCTRLPVK NKIIMLSFNL RICGMSSEAD RLEELVEYLE QSNGIQISDL HAVLELLVEL S GTGPPQLL PPKRDYFKNN KYVGRNVKYQ GYDYYDVQVF EADLGTTVAY QELEISTTIQ RT LQIMEAA PGTGLPALSF FSQNDLSTDK FEKETRGSLF GALVHSRTND MDIKLDMPPV PEN ADLSGL AIKVPQSIDQ SEDEGFQSAS NMTPDSQSEP SMTPDIDVWE AVLTYGPSKR RCWE RIGCP PGKREEPYVT EAGREAFDKL YKLHEGGLQI LSATTLQPQL VLLEETDLVK AVLNV LIGV VSSTFSYNQA LQSFAVKQGV YISGTSPDNV SSLLTQVAEY GTYYTRLSHF SLLTVL DSS HSNGLVFQAF TSGLRKYLQY YRACVLSTPA SLTLLTISFL FRKLGRQLRY LAELCCI GT LVTSATRGIS TAFPTGVKLL SYLYKEALEN SSNENYPVLL SLLKTSCEPY TRFIYDWV Y SGVFRDVCGE FMIQVNEDYL GFRDKRYWTH GYVLISKEVE DCVPVFLKHV ANEIYICGK TINLLKLCCP KHYICWSDIP VPRISVTFSL EELKEMEKDC AVYVARMERI ARHSCISKEQ KALQTEIAR QELIIQARET TEKVFETFKD RKLAEKLSLD TKKRELFQKL KDQYEKEQER R LTTKQEEA DDDFSYAREI RDREKRLKAL EEELELKTRQ ELIEHYSRLS EEATRKEQRA LW KLQRHKL ETIRLKFFLE EQKRMQDLVA NFPVDICEEN LGVLPDGEIS HQTDNTNDAG LGN IENEKS VPEQHALHNN NDEVYTAQNC ISKSESLCVD VTLPTENVHS QTSNASVLGV PSFD SNLCT PDVDIIDFLP TLPSENQEVA VVQSLVDDAL ISIGSDLNTD TKDKESLCAL KSDLQ ESST GSEYDFKTIL KPIACTQVSQ GHIKIGEYSS NVQPARPRWS THGHSSDSNI KIGNYV SDI NVHQPKHSQH GHSSDSNINI SDHMSDVEPR LPRLNLHGHI STGHIKVGEY ASDVEPS TP RHSVHGHASQ GNIKIGENVS DVKLSRPRWN IHGHVSDANI KIGENTSEIA PLRPRWNI H GHASQSHIKI GELVSDIEPS QPRRTPFGHP SQSSIPIGDQ PVEKYAQKSE SEVHSSNST IQHLLYSNIP DKNKDTGGTL TDSPVPVPDQ GNSNDDTEKR SSTLEQRVQA ADSVCDGEAS PNTAQSLPC MSDTLDFGTN GEENVGNDDH TWEKQQEYLK GLAEKYCLEK YQDSYELMSH P PVLHLYSN VMPNRFSFPT DSDIKSATDE TTVQLIELLS LPVLMKYSVT APMVSHVYLV NK AIVDYYF VELKMERHFE AMRHFLLMED GEFAQSLSDM LFEKLGSGQT PSELLNPLVL NSI LNKALQ YSLHGDSSLA SNLTFALKYL PEVFTPTAPD ALSCLELKYK VDWPLNIVIT DTCM NKYSR IFSFLLQLKH MVWTLRDVWF HLKRTALVNQ ASNSVQYRQL QLYRHEMQHF VKVIQ GYIA NQILHVTWCE FRNKLSAVSN LEEIYKTHAD YLNKALFRGL LTEKAAPLMN IIHSIF SLI LKFRLQLISQ SWICDTGKQM AVHPNFGLMQ QSYNTFKYYS DFLFEVVSKL VNRGYQP HL EDFLLRINFN SYYKQS UniProtKB: Gamma-tubulin complex component 6 |
-Macromolecule #5: Gamma-tubulin complex component 5
Macromolecule | Name: Gamma-tubulin complex component 5 / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: MAHWTRFERD QEGDIKKLVS LMSGIQDDQD GNFQQALQFA WSNFRFHRYL DVSSHTVLRT LEGIFEKLV VHSDLEKAES WKRLTEEFLL LPLPNTEGTK TDSHFAVLSL LLCLSDSPSN H DYTEKPRK KENDEQEPFD WGKYLREGED IEFSPDADTP EWSEASEEED ...String: MAHWTRFERD QEGDIKKLVS LMSGIQDDQD GNFQQALQFA WSNFRFHRYL DVSSHTVLRT LEGIFEKLV VHSDLEKAES WKRLTEEFLL LPLPNTEGTK TDSHFAVLSL LLCLSDSPSN H DYTEKPRK KENDEQEPFD WGKYLREGED IEFSPDADTP EWSEASEEED AQEPPSREDS GI QVDRTPL EDPEKKGAPP LVSWKVGEPD ARSWLEQHIV HQYWTSRAPR FSHSSHLHSN LSA IWDQHL YTTDPLYTPD DKTIVTETQV IRETLWLLSG VKKLLIFQLN DGKVNVRNDI IVTH MTQNC LRSVLEQIAA YGQVVFRLQK FIDEITGHGS EVPLPGTLPT AKKTTEAPFR TYQAF MWAL YKYFISFKEE LTEIEKCIIN KDETVTLAIV LDKLAPRLAQ LKVLHRVFST GIAEVP PDT RNVVRASHLL NTLYKAILDY DNVGEASEQT VSLLFCLWVE TVRPYLEIVD EWIVHGN LF DPAKEFIIQR NKDVPFNHRD FWYATYTLYS VSEKTENEDK MSDNASASSG SDQAPAGR Q HTMVSFLKPV LKQIIMAGKS MQLLKNLKCR TALQQDSSRD SDRKSLYTLF LESVQSRLQ HGNDSVPDII TEQQVNKLSL IKMQSIVAKH LELDEVHDPL LAINFVRLYL EQSDFLETFT CNEVCVDRS SESVTCQSFE LTLRSCLYPH IGKQYLECCG NLMYTLKKDY RLVEYLQAMR N FFLLEAGD TMYDFYTPIF DKIREKEPWL NLSYLNVQIQ EAVGQRYPDD STRLSVSFES VD LAKKKLP VHTLDGLILS YKVPWPVDIV ISSECQKIYN QVFLLLLLIK WAKYSLDVLQ FNE LGNASE NESTKEGATV EPFPLPPLTS PSEPKGQQIH RMFLLRVKLM HFVNSLHNYL MTRI LHSTG LEFQHQVEEA KDLDQLIKIH YRYLSTIHDR CLLREKVSSV KEAIMKVLNV VLMFA DRWH AGLGAWKKES IVKMESDFTN CHKFLVKVLN KAVCRGSFPH LESLALSLMA GMEQS UniProtKB: Gamma-tubulin complex component |
-Macromolecule #6: Mitotic-spindle organizing protein 1
Macromolecule | Name: Mitotic-spindle organizing protein 1 / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: MANASGNMSA VRETMDVLLE ISRLLNTGLD METLSICVRL CEQGINPEAL SSVIKELRRA SDTLKASES TAS UniProtKB: Mitotic-spindle organizing protein 1 |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 8 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 51.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: EMDB MAP EMDB ID: Details: The reference contains no density for the NEDD1/N-GCP/MZT1 grapnel and density for the GRIP2 domains and gamma-tubulins at spokes 5 and 6 was removed |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 7.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 82813 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |