Browse by MODEL: Ab initio only

SASDQB5 – Elongation factor Tu from Mycobacterium tuberculosis

Elongation factor Tu experimental SAS data
DAMMIN model
Sample: Elongation factor Tu monomer, 44 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jul 12
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis. Commun Biol 5(1):1052 (2022)
Zhan B, Gao Y, Gao W, Li Y, Li Z, Qi Q, Lan X, Shen H, Gan J, Zhao G, Li J
RgGuinier 3.5 nm
Dmax 9.0 nm
VolumePorod 94 nm3

SASDQC5 – Elongation factor Ts from Mycobacterium tuberculosis

Elongation factor Ts experimental SAS data
DAMMIN model
Sample: Elongation factor Ts monomer, 29 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jul 12
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis. Commun Biol 5(1):1052 (2022)
Zhan B, Gao Y, Gao W, Li Y, Li Z, Qi Q, Lan X, Shen H, Gan J, Zhao G, Li J
RgGuinier 2.7 nm
Dmax 10.1 nm
VolumePorod 46 nm3

SASDQD5 – Elongation factor-Tu and Elongation factor-Ts complex from Mycobacterium tuberculosis

Elongation factor TuElongation factor Ts experimental SAS data
DAMMIN model
Sample: Elongation factor Tu monomer, 44 kDa Mycobacterium tuberculosis (strain … protein
Elongation factor Ts monomer, 29 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jul 12
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis. Commun Biol 5(1):1052 (2022)
Zhan B, Gao Y, Gao W, Li Y, Li Z, Qi Q, Lan X, Shen H, Gan J, Zhao G, Li J
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 111 nm3

SASDP79 – Chromatin assembly factor 1 - long alpha-helix domain

Chromatin assembly factor 1 subunit A experimental SAS data
DAMMIN model
Sample: Chromatin assembly factor 1 subunit A monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 200 mM NaCl, 0.1 mM TCEP, pH: 7
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2021 Oct 28
Unorthodox PCNA Binding by Chromatin Assembly Factor 1 International Journal of Molecular Sciences 23(19):11099 (2022)
Gopinathan Nair A, Rabas N, Lejon S, Homiski C, Osborne M, Cyr N, Sverzhinsky A, Melendy T, Pascal J, Laue E, Borden K, Omichinski J, Verreault A
RgGuinier 4.1 nm
Dmax 17.2 nm
VolumePorod 54 nm3

SASDNM3 – Sperm-expressed surface protein

Sperm acrosome membrane-associated protein 6 experimental SAS data
DAMFILT model
Sample: Sperm acrosome membrane-associated protein 6 monomer, 25 kDa Homo sapiens protein
Buffer: 2.7 mM KCl, 137 mM NaCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH: 7.4
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2021 Dec 11
SPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins. Commun Biol 5(1):984 (2022)
Vance TDR, Yip P, Jiménez E, Li S, Gawol D, Byrnes J, Usón I, Ziyyat A, Lee JE
RgGuinier 3.0 nm
Dmax 9.5 nm
VolumePorod 34 nm3

SASDNQ5 – Meiosis protein TEX12 (Testis-expressed protein 12) – L110E, F114E, I117E, L121E mutant

Testis-expressed protein 12 (L110E, F114E, I117E, L121E) experimental SAS data
DAMMIF model
Sample: Testis-expressed protein 12 (L110E, F114E, I117E, L121E) tetramer, 36 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Sep 15
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip Communications Biology 5(1) (2022)
Dunce J, Salmon L, Davies O
RgGuinier 3.3 nm
Dmax 12.9 nm
VolumePorod 59 nm3

SASDMX6 – 40-mer single stranded DNA inhibitor of DNA dC->dU-editing enzyme APOBEC3G

40-mer single stranded inhibitory DNA experimental SAS data
DAMFILT model
Sample: 40-mer single stranded inhibitory DNA monomer, 12 kDa DNA
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 8
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 3.2 nm
Dmax 11.8 nm
VolumePorod 26 nm3

SASDMY6 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length

DNA dC->dU-editing enzyme APOBEC-3G experimental SAS data
DAMFILT model
Sample: DNA dC->dU-editing enzyme APOBEC-3G tetramer, 186 kDa Homo sapiens protein
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 4.2 nm
Dmax 13.3 nm
VolumePorod 350 nm3

SASDMZ6 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length in complex with DNA: tetramer

DNA dC->dU-editing enzyme APOBEC-3G40-mer single stranded inhibitory DNA experimental SAS data
DAMFILT model
Sample: DNA dC->dU-editing enzyme APOBEC-3G tetramer, 186 kDa Homo sapiens protein
40-mer single stranded inhibitory DNA dimer, 24 kDa DNA
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 4.7 nm
Dmax 16.2 nm
VolumePorod 395 nm3

SASDM27 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length in complex with DNA: monomer

40-mer single stranded inhibitory DNADNA dC->dU-editing enzyme APOBEC-3G experimental SAS data
DAMFILT model
Sample: 40-mer single stranded inhibitory DNA monomer, 12 kDa DNA
DNA dC->dU-editing enzyme APOBEC-3G monomer, 46 kDa Homo sapiens protein
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 118 nm3