SASBDB entries for UniProt ID: P35609

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

SASDZJ4 – Alpha-actinin-2 (ACTN2) wild-type, SEC-SAXS (aggregate peak)

UniProt ID: P35609 (None-None) Alpha-actinin-2
Alpha-actinin-2 experimental SAS data
Alpha-actinin-2 Kratky plot
Sample: Alpha-actinin-2 dimer, 208 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 13
Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun 17(1) (2026)
Noureddine M, Mikolajek H, Cowieson N, Pinotsis N, Robinson P, Slater A, Redwood C, Loughna S, Denning C, Mohammed F, Gehmlich K
RgGuinier 12.1 nm
Dmax 40.6 nm

SASDZK4 – Alpha-actinin-2 (ACTN2) wild-type, SEC-SAXS (dimer peak)

UniProt ID: P35609 (None-None) Alpha-actinin-2
Alpha-actinin-2 experimental SAS data
Alpha-actinin-2 Kratky plot
Sample: Alpha-actinin-2 dimer, 208 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 13
Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun 17(1) (2026)
Noureddine M, Mikolajek H, Cowieson N, Pinotsis N, Robinson P, Slater A, Redwood C, Loughna S, Denning C, Mohammed F, Gehmlich K
RgGuinier 11.9 nm
Dmax 36.2 nm

SASDZL4 – ACTN2-R457C at 60 degrees (°C) using batch-mode SAXS

UniProt ID: P35609 (None-None) Alpha-actinin-2
Alpha-actinin-2 experimental SAS data
Alpha-actinin-2 Kratky plot
Sample: Alpha-actinin-2 dimer, 208 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 13
Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun 17(1) (2026)
Noureddine M, Mikolajek H, Cowieson N, Pinotsis N, Robinson P, Slater A, Redwood C, Loughna S, Denning C, Mohammed F, Gehmlich K
RgGuinier 10.9 nm
Dmax 37.0 nm

SASDZM4 – ACTN2-R457C at 53 degrees (°C) using batch-mode SAX

UniProt ID: P35609 (None-None) Alpha-actinin-2
Alpha-actinin-2 experimental SAS data
Alpha-actinin-2 Kratky plot
Sample: Alpha-actinin-2 dimer, 208 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 13
Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun 17(1) (2026)
Noureddine M, Mikolajek H, Cowieson N, Pinotsis N, Robinson P, Slater A, Redwood C, Loughna S, Denning C, Mohammed F, Gehmlich K
RgGuinier 10.3 nm
Dmax 35.3 nm

SASDZN4 – ACTN2-R457C at 40 degrees (°C) using batch-mode SAXS

UniProt ID: P35609 (None-None) Alpha-actinin-2
Alpha-actinin-2 experimental SAS data
Alpha-actinin-2 Kratky plot
Sample: Alpha-actinin-2 dimer, 208 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 13
Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun 17(1) (2026)
Noureddine M, Mikolajek H, Cowieson N, Pinotsis N, Robinson P, Slater A, Redwood C, Loughna S, Denning C, Mohammed F, Gehmlich K
RgGuinier 10.3 nm
Dmax 37.0 nm

SASDZP4 – ACTN2-E448A at 60 degrees (°C) using batch-mode SAXS

UniProt ID: P35609 (None-None) Alpha-actinin-2
Alpha-actinin-2 experimental SAS data
Alpha-actinin-2 Kratky plot
Sample: Alpha-actinin-2 dimer, 208 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 May 13
Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun 17(1) (2026)
Noureddine M, Mikolajek H, Cowieson N, Pinotsis N, Robinson P, Slater A, Redwood C, Loughna S, Denning C, Mohammed F, Gehmlich K
RgGuinier 10.9 nm
Dmax 36.9 nm