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- EMDB-48669: Focused map of Pfs230 domains 1-8 of the endogenous Pfs230-Pfs48/... -

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Basic information

Entry
Database: EMDB / ID: EMD-48669
TitleFocused map of Pfs230 domains 1-8 of the endogenous Pfs230-Pfs48/45 complex
Map dataLocal refinement of map corresponding to Pfs230 D1-D8
Sample
  • Complex: Heterodimeric complex of endogenous Plasmodium falciparum proteins Pfs230 and Pfs48/45
    • Protein or peptide: Gametocyte surface protein P230
Keywords6-cysteine protein / Plasmodium falciparum / malaria transmission / protein binding
Function / homology: / 6-Cysteine (6-Cys) domain / 6-Cysteine (6-Cys) domain superfamily / Sexual stage antigen s48/45 domain / 6-Cysteine (6-Cys) domain profile. / Sexual stage antigen s48/45 domain / cell surface / plasma membrane / Gametocyte surface protein P230
Function and homology information
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.86 Å
AuthorsDietrich MH / Glukhova A / Shakeel S / Tham WH
Funding support Australia, 2 items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP2001385 Australia
National Health and Medical Research Council (NHMRC, Australia)APP2016908 Australia
CitationJournal: To Be Published
Title: Cryo-EM structure of the native Pfs230 and Pfs48/45 fertilization complex from Plasmodium falciparum
Authors: Dietrich MH / Chmielewski J / Chan LJ / Tan LL / Adair A / Lyons FMT / Gabriela M / Lopaticki S / Dite TA / Dagley LF / Longley R / Mueller I / Glukhova A / Shakeel S / Tham WH
History
DepositionJan 16, 2025-
Header (metadata) releaseJul 30, 2025-
Map releaseJul 30, 2025-
UpdateJul 30, 2025-
Current statusJul 30, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_48669.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationLocal refinement of map corresponding to Pfs230 D1-D8
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.81 Å/pix.
x 360 pix.
= 290.88 Å
0.81 Å/pix.
x 360 pix.
= 290.88 Å
0.81 Å/pix.
x 360 pix.
= 290.88 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.808 Å
Density
Contour LevelBy AUTHOR: 0.0285
Minimum - Maximum-0.1658827 - 0.5768393
Average (Standard dev.)0.00027542526 (±0.0061783902)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 290.88 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_48669_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_48669_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_48669_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Heterodimeric complex of endogenous Plasmodium falciparum protein...

EntireName: Heterodimeric complex of endogenous Plasmodium falciparum proteins Pfs230 and Pfs48/45
Components
  • Complex: Heterodimeric complex of endogenous Plasmodium falciparum proteins Pfs230 and Pfs48/45
    • Protein or peptide: Gametocyte surface protein P230

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Supramolecule #1: Heterodimeric complex of endogenous Plasmodium falciparum protein...

SupramoleculeName: Heterodimeric complex of endogenous Plasmodium falciparum proteins Pfs230 and Pfs48/45
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Plasmodium falciparum (malaria parasite P. falciparum)
Molecular weightTheoretical: 400 KDa

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Macromolecule #1: Gametocyte surface protein P230

MacromoleculeName: Gametocyte surface protein P230 / type: protein_or_peptide / ID: 1 / Details: Pfs230 domains 1 to 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Plasmodium falciparum (malaria parasite P. falciparum)
Molecular weightTheoretical: 363.70175 KDa
SequenceString: MKKIITLKNL FLIILVYIFS EKKDLRCNVI KGNNIKDDED KRFHLFYYSH NLFKTPETKE KKNKKECFYK NGGIYNLSKE IRMRKDTSV KIKQRTCPFH KEGSSFEMGS KNITCFYPIV GKKERKTLDT IIIKKNVTND HVVSSDMHSN VQEKNMILIR N IDKENKND ...String:
MKKIITLKNL FLIILVYIFS EKKDLRCNVI KGNNIKDDED KRFHLFYYSH NLFKTPETKE KKNKKECFYK NGGIYNLSKE IRMRKDTSV KIKQRTCPFH KEGSSFEMGS KNITCFYPIV GKKERKTLDT IIIKKNVTND HVVSSDMHSN VQEKNMILIR N IDKENKND IQNVEEKIQR DTYENKDYES DDTLIEWFDD NTNEENFLLT FLKRCLMKIF SSPKRKKTVV QKKHKSNFFI NS SLKYIYM YLTPSDSFNL VRRNRNLDEE DMSPRDNFVI DDEEEEEEEE EEEEEEEEEE EEEEEEEYDD YVYEESGDET EEQ LQEEHQ EEVGAESSEE SFNDEDEDSV EARDGDMIRV DEYYEDQDGD TYDSTIKNED VDEEVGEEVG EEVGEEVGEE VGEE VGEEV GEEVGEEVGE EEGEEVGEGV GEEVGEEEGE EVGEEEGEYV DEKERQGEIY PFGDEEEKDE GGESFTYEKS EVDKT DLFK FIEGGEGDDV YKVDGSKVLL DDDTISRVSK KHTARDGEYG EYGEAVEDGE NVIKIIRSVL QSGALPSVGV DELDKI DLS YETTESGDTA VSEDSYDKYA SNNTNKEYVC DFTDQLKPTE SGPKVKKCEV KVNEPLIKVK IICPLKGSVE KLYDNIE YV PKKSPYVVLT KEETKLKEKL LSKLIYGLLI SPTVNEKENN FKEGVIEFTL PPVVHKATVF YFICDNSKTE DDNKKGNR G IVEVYVEPYG NKINGCAFLD EDEEEEKYGN QIEEDEHNEK IKMKTFFTQN IYKKNNIYPC YMKLYSGDIG GILFPKNIK STTCFEEMIP YNKEIKWNKE NKSLGNLVNN SVVYNKEMNA KYFNVQYVHI PTSYKDTLNL FCSIILKEEE SNLISTSYLV YVSINEELN FSLFDFYESF VPIKKTIQVA QKNVNNKEHD YTCDFTDKLD KTVPSTANGK KLFICRKHLK EFDTFTLKCN V NKTQYPNI EIFPKTLKDK KEVLKLDLDI QYQMFSKFFK FNTQNAKYLN LYPYYLIFPF NHIGKKELKN NPTYKNHKDV KY FEQSSVL SPLSSADSLG KLLNFLDTQE TVCLTEKIRY LNLSINELGS DNNTFSVTFQ VPPYIDIKEP FYFMFGCNNN KGE GNIGIV ELLISKQEEK IKGCNFHESK LDYFNENISS DTHECTLHAY ENDIIGFNCL ETTHPNEVEV EVEDAEIYLQ PENC FNNVY KGLNSVDITT ILKNAQTYNI NNKKTPTFLK IPPYNLLEDV EISCQCTIKQ VVKKIKVIIT KNDTVLLKRE VQSES TLDD KIYKCEHENF INPRVNKTFD ENVEYTCNIK IENFFNYIQI FCPAKDLGIY KNIQMYYDIV KPTRVPQFKK FNNEEL HKL IPNSEMLHKT KEMLILYNEE KVDLLHFYVF LPIYIKDIYE FNIVCDNSKT MWKNQLGGKV IYHITVSKRE QKVKGCS FD NEHAHMFSYN KTNVKNCIID AKPKDLIGFV CPSGTLKLTN CFKDAIVHTN LTNINGILYL KNNLANFTYK HQFNYMEI P ALMDNDISFK CICVDLKKKK YNVKSPLGPK VLRALYKKLN IKFDNYVTGT DQNKYLMTYM DLHLSHKRNY LKELFHDLG KKKPADTDAN PESIIESLSI NESNESGPFP TGDVDAEHLI LEGYDTWESL YDEQLEEVIY NDIESLELKD IEQYVLQVNL KAPKLMMSA QIHNNRHVCD FSKNNLIVPE SLKKKEELGG NPVNIHCYAL LKPLDTLYVK CPTSKDNYEA AKVNISENDN E YELQVISL IEKRFHNFET LESKKPGNGD VVVHNGVVDT GPVLDNSTFE KYFKNIKIKP DKFFEKVINE YDDTEEEKDL ES ILPGAIV SPMKVLKKKD PFTSYAAFVV PPIVPKDLHF KVECNNTEYK DENQYISGYN GIIHIDISNS NRKINGCDFS TNN SSILTS SVKLVNGETK NCEININNNE VFGIICDNET NLDPEKCFHE IYSKDNKTVK KFREVIPNID IFSLHNSNKK KVAY AKVPL DYINKLLFSC SCKTSHTNTI GTMKVTLNKD EKEEEDFKTA QGIKHNNVHL CNFFDNPELT FDNNKIVLCK IDAEL FSEV IIQLPIFGTK NVEEGVQNEE YKKFSLKPSL VFDDNNNDIK VIGKEKNEVS ISLALKGVYG NRIFTFDKNG KKGEGI SFF IPPIKQDTDL KFIINETIDN SNIKQRGLIY IFVRKNVSEN SFKLCDFTTG STSLMELNSQ VKEKKCTVKI KKGDIFG LK CPKGFAIFPQ ACFSNVLLEY YKSDYEDSEH INYYIHKDKK YNLKPKDVIE LMDENFRELQ NIQQYTGISN ITDVLHFK N FNLGNLPLNF KNHYSTAYAK VPDTFNSIIN FSCNCYNPEK HVYGTMQVES DNRNFDNIKK NENVIKNFLL PNIEKYALL LDDEERQKKI KQQQEEEQQE QILKDQDDRL SRHDDYNKNH TYILYDSNEH ICDYEKNESL ISTLPNDTKK IQKSICKINA KALDVVTIK CPHTKNFTPK DYFPNSSLIT NDKKIVITFD KKNFVTYIDP TKKTFSLKDI YIQSFYGVSL DHLNQIKKIH E EWDDVHLF YPPHNVLHNV VLNNHIVNLS SALEGVLFMK SKVTGDETAT KKNTTLPTDG VSSILIPPYV KEDITFHLFC GK STTKKPN KKNTSLALIH IHISSNRNII HGCDFLYLEN QTNDAISNNN NNSYSIFTHN KNTENNLICD ISLIPKTVIG IKC PNKKLN PQTCFDEVYY VKQEDVPSKT ITADKYNTFS KDKIGNILKN AISINNPDEK DNTYTYLILP EKFEEELIDT KKVL ACTCD NKYIIHMKIE KSTMDKIKID EKKTIGKDIC KYDVTTKVAT CEIIDTIDSS VLKEHHTVHY SITLSRWDKL IIKYP TNEK THFENFFVNP FNLKDKVLYN YNKPINIEHI LPGAITTDIY DTRTKIKQYI LRIPPYVHKD IHFSLEFNNS LSLTKQ NQN IIYGNVAKIF IHINQGYKEI HGCDFTGKYS HLFTYSKKPL PNDDDICNVT IGNNTFSGFA CLSHFELKPN NCFSSVY DY NEANKVKKLF DLSTKVELDH IKQNTSGYTL SYIIFNKEST KLKFSCTCSS NYSNYTIRIT FDPNYIIPEP QSRAIIKY V DLQDKNFAKY LRKL

UniProtKB: Gametocyte surface protein P230

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.4 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.86 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 87061
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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