Browse by MODEL: Ab initio only

SASDFA2 – Urokinase plasminogen activator surface receptor, uPAR T51C-V70C, complex with urokinase-type plasminogen activator (Amino Terminal Fragment, ATF).

Urokinase plasminogen activator surface receptorUrokinase-type plasminogen activator (Amino Terminal Fragment) experimental SAS data
DAMMIN model
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
Urokinase-type plasminogen activator (Amino Terminal Fragment) monomer, 16 kDa Homo sapiens protein
Buffer: 20 mM PBS, 5 %(v/v) glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Dec 1
Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond? J Biol Chem (2019)
Leth JM, Mertens HDT, Leth-Espensen KZ, Jørgensen TJD, Ploug M
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 77 nm3

SASDFB2 – Urokinase plasminogen activator surface receptor, uPAR, K50C-V70C

Urokinase plasminogen activator surface receptor experimental SAS data
DAMMIN model
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
Buffer: 20 mM PBS, 5 %(v/v) glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 May 5
Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond? J Biol Chem (2019)
Leth JM, Mertens HDT, Leth-Espensen KZ, Jørgensen TJD, Ploug M
RgGuinier 2.5 nm
Dmax 9.3 nm
VolumePorod 66 nm3

SASDFC2 – Urokinase plasminogen activator surface receptor, uPAR K50C-V70C, complex with urokinase-type plasminogen activator (Amino Terminal Fragment, ATF).

Urokinase plasminogen activator surface receptorUrokinase-type plasminogen activator (Amino Terminal Fragment) experimental SAS data
DAMMIN model
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
Urokinase-type plasminogen activator (Amino Terminal Fragment) monomer, 16 kDa Homo sapiens protein
Buffer: 20 mM PBS, 5 %(v/v) glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 May 5
Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond? J Biol Chem (2019)
Leth JM, Mertens HDT, Leth-Espensen KZ, Jørgensen TJD, Ploug M
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 66 nm3

SASDET9 – Gliding motility protein MglB: A GAP of Myxococcus xanthus MglA

Gliding motility protein MglB experimental SAS data
GASBOR model
Sample: Gliding motility protein MglB dimer, 34 kDa Myxococcus xanthus protein
Buffer: 150 mM NaCl, 1 mM DTT, 20 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Oct 9
MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus. Nat Commun 10(1):5300 (2019)
Galicia C, Lhospice S, Varela PF, Trapani S, Zhang W, Navaza J, Herrou J, Mignot T, Cherfils J
RgGuinier 2.8 nm
Dmax 10.3 nm
VolumePorod 56 nm3

SASDE37 – Lysine-specific demethylase 5B, KDM5B, in HEPES buffer

Lysine-specific demethylase 5B experimental SAS data
DAMFILT model
Sample: Lysine-specific demethylase 5B monomer, 176 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 300 mM NaCl, 5% (v/v) glycerol, 1mM DTT, pH: 7.7
Experiment: SAXS data collected at Xenocs BioXolver L with GeniX3D, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Oct 24
Molecular architecture of the Jumonji C family histone demethylase KDM5B. Sci Rep 9(1):4019 (2019)
Dorosz J, Kristensen LH, Aduri NG, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M
RgGuinier 8.8 nm
Dmax 26.9 nm

SASDDG5 – Mammalian prion protein mRNA (PrP mRNA wild type)

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: Octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Nov 4
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 7.4 nm
Dmax 25.0 nm
VolumePorod 165 nm3

SASDDH5 – Mammalian prion protein mRNA (PrP mRNA wild type) with KCl

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: Octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 8.8 nm
Dmax 31.0 nm
VolumePorod 240 nm3

SASDDJ5 – Mammalian prion protein mRNA (PrP mRNA wild type) with LiCl

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: Octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM LiCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 9.0 nm
Dmax 31.0 nm
VolumePorod 225 nm3

SASDDK5 – Mammalian prion protein mRNA (PrP mRNA wild type) with KCl and pyridostatin (PDS)

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: Octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM KCl and 1 mM PDS, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 9.1 nm
Dmax 31.0 nm
VolumePorod 220 nm3

SASDDL5 – Mutant mammalian prion protein mRNA (octo-repeat PrP mRNA)

octo-repeat PrP mRNA mutant experimental SAS data
DAMFILT model
Sample: Octo-repeat PrP mRNA mutant dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 7.0 nm
Dmax 24.0 nm
VolumePorod 150 nm3