SASBDB entries for UniProt ID:

SASDJA6 – Complement C5

UniProt ID: P01031 (19-1676) Complement C5
Complement C5 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Complement C5 monomer, 186 kDa Homo sapiens protein
Buffer: 20mM Tris pH, 75mM NaCl, and 3% glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 12
The allosteric modulation of Complement C5 by knob domain peptides. Elife 10 (2021)
Macpherson A, Laabei M, Ahdash Z, Graewert MA, Birtley JR, Schulze ME, Crennell S, Robinson SA, Holmes B, Oleinikovas V, Nilsson PH, Snowden J, Ellis V, Mollnes TE, Deane CM, Svergun D, Lawson AD, van den Elsen JM
RgGuinier 4.8 nm
Dmax 17.6 nm
VolumePorod 392 nm3

SASDJB6 – Lactococcus phage Phi28 apo-gp11 encapsidation protein

UniProt ID: B1ABI1 (None-None) gp11 encapsidation protein
gp11 encapsidation protein experimental SAS data
OTHER model
Sample: Gp11 encapsidation protein decamer, 446 kDa Lactococcus phage Phi28 protein
Buffer: 100 mM NaCl, 25 mM HEPES, pH: 7.4
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2015 May 6
Lactococcus Phage ASCC Phi28 gp11
Mark White
RgGuinier 5.3 nm
Dmax 16.3 nm

SASDJC6 – Human Vitamin K-dependent protein C

UniProt ID: P04070 (43-461) Vitamin K-dependent protein C
Vitamin K-dependent protein C experimental SAS data
DAMFILT model
Sample: Vitamin K-dependent protein C monomer, 62 kDa Homo sapiens protein
Buffer: 20 mM Tris, 145 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Jul 14
Zymogen and activated protein C have similar structural architecture. J Biol Chem (2020)
Stojanovski BM, Pelc LA, Zuo X, Di Cera E
RgGuinier 3.6 nm
Dmax 14.0 nm

SASDJD6 – Human Vitamin K-dependent Activated Protein C

UniProt ID: P04070 (43-461) Vitamin K-dependent protein C
Vitamin K-dependent protein C experimental SAS data
DAMFILT model
Sample: Vitamin K-dependent protein C monomer, 62 kDa Homo sapiens protein
Buffer: 20 mM Tris, 145 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Aug 17
Zymogen and activated protein C have similar structural architecture. J Biol Chem (2020)
Stojanovski BM, Pelc LA, Zuo X, Di Cera E
RgGuinier 3.7 nm
Dmax 14.0 nm

SASDJJ6 – Sarcomeric intrinsically disordered protein FATZ-1 (N-FATZ-1)

UniProt ID: Q9NP98 (1-174) N-ter construct of FATZ-1 (alias myozenin-1 or calsarcin-2)
N-ter construct of FATZ-1 (alias myozenin-1 or calsarcin-2) experimental SAS data
Sarcomeric intrinsically disordered protein FATZ-1 (N-FATZ-1) Rg histogram
Sample: N-ter construct of FATZ-1 (alias myozenin-1 or calsarcin-2) monomer, 20 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 29
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. Sci Adv 7(22) (2021)
Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K
RgGuinier 3.5 nm
Dmax 14.1 nm
VolumePorod 46 nm3

SASDJK6 – Sarcomeric intrinsically disordered protein FATZ-1 (Δ91-FATZ-1)

UniProt ID: Q9NP98 (92-299) Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2)
Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2) experimental SAS data
Sarcomeric intrinsically disordered protein FATZ-1 (Δ91-FATZ-1) Rg histogram
Sample: Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2) monomer, 22 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 18
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. Sci Adv 7(22) (2021)
Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K
RgGuinier 3.9 nm
Dmax 17.3 nm
VolumePorod 66 nm3

SASDJL6 – Sarcomeric F-actin crosslinking protein α-actinin-2 (spectrin repeat rod domain, rod-α-actinin-2)

UniProt ID: P35609 (274-746) Rod domain of α-actinin-2
Rod domain of α-actinin-2 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Rod domain of α-actinin-2 dimer, 112 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Dec 5
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. Sci Adv 7(22) (2021)
Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K
RgGuinier 6.7 nm
Dmax 27.2 nm
VolumePorod 214 nm3

SASDJM6 – Sarcomeric F-actin crosslinking protein α-actinin-2 (half-dimer, hd)

UniProt ID: P35609 (1-894) Half dimer of α-actinin-2
Half dimer of α-actinin-2 experimental SAS data
Sarcomeric F-actin crosslinking protein α-actinin-2 (half-dimer, hd) Rg histogram
Sample: Half dimer of α-actinin-2 monomer, 107 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 18
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. Sci Adv 7(22) (2021)
Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K
RgGuinier 5.3 nm
Dmax 22.0 nm
VolumePorod 172 nm3

SASDJN6 – Sarcomeric fuzzy α-actinin-2/FATZ-1 complex (rod-α-actinin-2/Δ91-FATZ-1)

UniProt ID: P35609 (274-746) Rod domain of α-actinin-2

UniProt ID: Q9NP98 (92-299) Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2)
Rod domain of α-actinin-2Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2) experimental SAS data
Sarcomeric fuzzy α-actinin-2/FATZ-1 complex (rod-α-actinin-2/Δ91-FATZ-1) Rg histogram
Sample: Rod domain of α-actinin-2 dimer, 112 kDa Homo sapiens protein
Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2) dimer, 43 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 18
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. Sci Adv 7(22) (2021)
Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K
RgGuinier 7.6 nm
Dmax 28.4 nm
VolumePorod 371 nm3

SASDJP6 – Sarcomeric fuzzy α-actinin-2/FATZ-1 complex (hd-α-actinin-2/Δ91-FATZ-1)

UniProt ID: Q9NP98 (92-299) Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2)

UniProt ID: P35609 (1-894) Half dimer of α-actinin-2
Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2)Half dimer of α-actinin-2 experimental SAS data
Sarcomeric fuzzy α-actinin-2/FATZ-1 complex (hd-α-actinin-2/Δ91-FATZ-1) Rg histogram
Sample: Δ91 construct of FATZ-1 (alias myozenin-1 or calsarcin-2) monomer, 22 kDa Homo sapiens protein
Half dimer of α-actinin-2 monomer, 107 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 18
Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. Sci Adv 7(22) (2021)
Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K
RgGuinier 5.8 nm
Dmax 22.5 nm
VolumePorod 242 nm3