Browse by MODEL: No model

SASDLU6 – Complex glycan contactin 1 ectodomain, 2.5 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 8.0 nm
Dmax 25.7 nm
VolumePorod 350 nm3

SASDLV6 – High mannose glycan contactin 1 ectodomain, 20.5 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 7.0 nm
Dmax 34.0 nm
VolumePorod 285 nm3

SASDLW6 – High mannose glycan contactin 1 ectodomain, 11.1 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 27.0 nm
VolumePorod 275 nm3

SASDLX6 – High mannose glycan contactin 1 ectodomain, 5.5 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 27.0 nm
VolumePorod 270 nm3

SASDQN5 – Candida glabrata Metacaspase in 10 mM CaCl2

Metacaspase-1 experimental SAS data
Metacaspase-1 Kratky plot
Sample: Metacaspase-1 monomer, 46 kDa Candida glabrata (strain … protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1% glycerol, 10 mM CaCl2, pH: 7.6
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 26
Structural and molecular determinants of Candida glabrata metacaspase maturation and activation by calcium. Commun Biol 5(1):1158 (2022)
Conchou L, Doumèche B, Galisson F, Violot S, Dugelay C, Diesis E, Page A, Bienvenu AL, Picot S, Aghajari N, Ballut L
RgGuinier 1.9 nm
Dmax 5.4 nm
VolumePorod 43 nm3

SASDNU7 – Obscurin Ig domains 12/13 at neutral pH

Obscurin experimental SAS data
Obscurin Kratky plot
Sample: Obscurin monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 0.35 mM NaN3, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 May 18
The N-terminus of obscurin is flexible in solution. Proteins (2022)
Mauriello GE, Moncure GE, Nowzari RA, Miller CJ, Wright NT
RgGuinier 2.8 nm
Dmax 10.5 nm
VolumePorod 28 nm3

SASDNV7 – Obscurin Ig domains 11/12 at neutral pH

Obscurin experimental SAS data
Obscurin Kratky plot
Sample: Obscurin monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 0.35 mM NaN3, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Nov 18
The N-terminus of obscurin is flexible in solution. Proteins (2022)
Mauriello GE, Moncure GE, Nowzari RA, Miller CJ, Wright NT
RgGuinier 3.7 nm
Dmax 18.0 nm
VolumePorod 66 nm3

SASDPE8 – SMARCA2 bromodomain (isoform1):Protac (ACBI1):VCB (VHL-elongin C-elongin B)

Probable global transcription activator SNF2L2 (isoform 1)von Hippel-Lindau disease tumor suppressorElongin-BElongin-CACBI1 protac experimental SAS data
Probable global transcription activator SNF2L2 (isoform 1) von Hippel-Lindau disease tumor suppressor Elongin-B Elongin-C ACBI1 protac Kratky plot
Sample: Probable global transcription activator SNF2L2 (isoform 1) monomer, 16 kDa Homo sapiens protein
Von Hippel-Lindau disease tumor suppressor monomer, 19 kDa Homo sapiens protein
Elongin-B monomer, 12 kDa Homo sapiens protein
Elongin-C monomer, 11 kDa Homo sapiens protein
ACBI1 protac monomer, 1 kDa
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2021 Aug 11
Predicting the structural basis of targeted protein degradation by integrating molecular dynamics simulations with structural mass spectrometry. Nat Commun 13(1):5884 (2022)
Dixon T, MacPherson D, Mostofian B, Dauzhenka T, Lotz S, McGee D, Shechter S, Shrestha UR, Wiewiora R, McDargh ZA, Pei F, Pal R, Ribeiro JV, Wilkerson T, Sachdeva V, Gao N, Jain S, Sparks S, Li Y, Vinitsky A, Zhang X, Razavi AM, Kolossváry I, Imbriglio J, Evdokimov A, Bergeron L, Zhou W, Adhikari J, Ruprecht B, Dickson A, Xu H, Sherman W, Izaguirre JA
RgGuinier 3.3 nm
Dmax 12.5 nm
VolumePorod 83 nm3

SASDPF8 – SMARCA2 bromodomain (isoform2):Protac (ACBI1):VCB (VHL-elongin C-elongin B)

von Hippel-Lindau disease tumor suppressorElongin-BElongin-CACBI1 protacProbable global transcription activator SNF2L2 (isoform 2) experimental SAS data
von Hippel-Lindau disease tumor suppressor Elongin-B Elongin-C ACBI1 protac Probable global transcription activator SNF2L2 (isoform 2) Kratky plot
Sample: Von Hippel-Lindau disease tumor suppressor monomer, 19 kDa Homo sapiens protein
Elongin-B monomer, 12 kDa Homo sapiens protein
Elongin-C monomer, 11 kDa Homo sapiens protein
ACBI1 protac monomer, 1 kDa
Probable global transcription activator SNF2L2 (isoform 2) monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2021 Aug 11
Predicting the structural basis of targeted protein degradation by integrating molecular dynamics simulations with structural mass spectrometry. Nat Commun 13(1):5884 (2022)
Dixon T, MacPherson D, Mostofian B, Dauzhenka T, Lotz S, McGee D, Shechter S, Shrestha UR, Wiewiora R, McDargh ZA, Pei F, Pal R, Ribeiro JV, Wilkerson T, Sachdeva V, Gao N, Jain S, Sparks S, Li Y, Vinitsky A, Zhang X, Razavi AM, Kolossváry I, Imbriglio J, Evdokimov A, Bergeron L, Zhou W, Adhikari J, Ruprecht B, Dickson A, Xu H, Sherman W, Izaguirre JA
RgGuinier 3.2 nm
Dmax 11.1 nm
VolumePorod 75 nm3

SASDPF7 – Ribonuclease A SEC-SAXS data (EMBL-P12 bioSAXS beam line at DESY)

Ribonuclease pancreatic experimental SAS data
Ribonuclease pancreatic Kratky plot
Sample: Ribonuclease pancreatic monomer, 14 kDa Bos taurus protein
Buffer: 50 mM HEPES, 150 mM KCl, 3% glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 16
Small-Angle X-ray Scattering data (benchmarking/consensus): EMBL-P12 SAXS beam line, DESY
Clement Blanchet, Melissa Graewert, Cy M Jeffries, Dmitri Svergun
RgGuinier 1.5 nm
Dmax 4.6 nm
VolumePorod 16 nm3