Browse by ORGANISM: Homo sapiens (Human)

SASDF28 – Myotilin immunoglobulin domains Ig1Ig2 (220-452)

Myotilin Ig1Ig2 (220-452) experimental SAS data
Myotilin Ig1Ig2 (220-452) Kratky plot
Sample: Myotilin Ig1Ig2 (220-452) monomer, 27 kDa Homo sapiens protein
Buffer: 20 mM Na+-HEPES, 150 mM, NaCl, 5 % v/v glycerol, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2010 Nov 16
Molecular basis of F-actin regulation and sarcomere assembly via myotilin PLOS Biology 19(4):e3001148 (2021)
Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M, Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L
RgGuinier 3.7 nm
Dmax 15.1 nm
VolumePorod 52 nm3

SASDF38 – Myotilin immunoglobulin domains Ig1Ig2 (250-444)

Myotilin Ig1Ig2 (250-444) experimental SAS data
Myotilin Ig1Ig2 (250-444) Kratky plot
Sample: Myotilin Ig1Ig2 (250-444) monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Na+-HEPES, 150 mM, NaCl, 5 % v/v glycerol, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2019 Jun 27
Molecular basis of F-actin regulation and sarcomere assembly via myotilin PLOS Biology 19(4):e3001148 (2021)
Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M, Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L
RgGuinier 2.8 nm
Dmax 10.1 nm
VolumePorod 29 nm3

SASDF48 – Myotilin immunoglobulin domains Ig1Ig2 (250-498)

Myotilin Ig1Ig2 (250-498) experimental SAS data
Myotilin Ig1Ig2 (250-498) Kratky plot
Sample: Myotilin Ig1Ig2 (250-498) monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Na+-HEPES, 150 mM, NaCl, 5 % v/v glycerol, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2019 Jun 27
Molecular basis of F-actin regulation and sarcomere assembly via myotilin PLOS Biology 19(4):e3001148 (2021)
Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M, Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L
RgGuinier 3.2 nm
Dmax 14.0 nm
VolumePorod 37 nm3

SASDJH8 – Myotilin immunoglobulin domains Ig1Ig2 (220-452, wild-type) concentration series data

Myotilin (222-452) experimental SAS data
Myotilin (222-452) Kratky plot
Sample: Myotilin (222-452) monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 % glycerol, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jul 6
Molecular basis of F-actin regulation and sarcomere assembly via myotilin PLOS Biology 19(4):e3001148 (2021)
Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M, Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L
RgGuinier 3.3 nm
Dmax 11.5 nm
VolumePorod 36 nm3

SASDJJ8 – Myotilin immunoglobulin domains Ig1Ig2 (220-452, R405K mutant) concentration series data

Myotilin (222-452) R405K experimental SAS data
Myotilin (222-452) R405K Kratky plot
Sample: Myotilin (222-452) R405K monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 % glycerol, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jul 12
Molecular basis of F-actin regulation and sarcomere assembly via myotilin PLOS Biology 19(4):e3001148 (2021)
Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M, Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L
RgGuinier 3.3 nm
Dmax 10.5 nm
VolumePorod 36 nm3

SASDJU4 – X-ray repair cross-complementing proteins 5 and 6

X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5 experimental SAS data
BILBOMD model
Sample: X-ray repair cross-complementing protein 6 monomer, 70 kDa Homo sapiens protein
X-ray repair cross-complementing protein 5 monomer, 83 kDa Homo sapiens protein
Buffer: 50 mM Hepes, 50 mM KCl, 5 mM MgCl2, 5% glycerol and 0.2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 12
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog Biophys Mol Biol (2020)
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA
RgGuinier 4.2 nm
Dmax 14.9 nm
VolumePorod 253 nm3

SASDJV4 – X-ray repair cross-complementing proteins 5ΔCTR and 6

X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5 ΔCTR experimental SAS data
BILBOMD model
Sample: X-ray repair cross-complementing protein 6 monomer, 70 kDa Homo sapiens protein
X-ray repair cross-complementing protein 5 ΔCTR monomer, 64 kDa Homo sapiens protein
Buffer: 50 mM Hepes, 50 mM KCl, 5 mM MgCl2, 5% glycerol and 0.2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 12
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog Biophys Mol Biol (2020)
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 240 nm3

SASDJW4 – X-ray repair cross-complementing proteins 5 and 6-DNA

X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5Y-DNA experimental SAS data
BILBOMD model
Sample: X-ray repair cross-complementing protein 6 monomer, 70 kDa Homo sapiens protein
X-ray repair cross-complementing protein 5 monomer, 83 kDa Homo sapiens protein
Y-DNA monomer, 18 kDa DNA
Buffer: 50 mM Tris-HCl, 100 mM NaCl, 5% glycerol, 0.01% sodium azide, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2010 Jan 8
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog Biophys Mol Biol (2020)
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA
RgGuinier 4.1 nm
Dmax 14.8 nm
VolumePorod 280 nm3

SASDJX4 – DNA-dependent protein kinase catalytic subunit (DNA-PKcs)

DNA-dependent protein kinase catalytic subunit experimental SAS data
BILBOMD model
Sample: DNA-dependent protein kinase catalytic subunit monomer, 468 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl, 5% glycerol, 0.01% sodium azide, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Dec 30
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog Biophys Mol Biol (2020)
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA
RgGuinier 5.6 nm
Dmax 15.6 nm
VolumePorod 1040 nm3

SASDJY4 – Autophosphorylated DNA-dependent protein kinase (DNA-PKcs)

DNA-dependent protein kinase catalytic subunit experimental SAS data
BILBOMD model
Sample: DNA-dependent protein kinase catalytic subunit monomer, 468 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 100 mM KCl, 5% (v/v) glycerol, 0.2 mM EDTA containing 0.1 mM benzamidine, 0.2 mM PMSF and 0.2 µg/ml pepstatin, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2010 Jan 8
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog Biophys Mol Biol (2020)
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA
RgGuinier 5.5 nm
Dmax 16.1 nm
VolumePorod 918 nm3