|
|
|
|
|
| Sample: |
Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
DNA (ACTCCTTTTT) monomer, 1 kDa DNA
|
| Buffer: |
20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7 |
| Experiment: |
SAXS
data collected at SAXS/WAXS, Australian Synchrotron on 2016 May 27
|
TIA-1 RRM23 binding and recognition of target oligonucleotides.
Nucleic Acids Res 45(8):4944-4957 (2017)
Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA
|
| RgGuinier |
2.2 |
nm |
| Dmax |
6.7 |
nm |
| VolumePorod |
32 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
DNA (TTTTTACTCC) monomer, 1 kDa DNA
|
| Buffer: |
20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7 |
| Experiment: |
SAXS
data collected at SAXS/WAXS, Australian Synchrotron on 2016 May 27
|
TIA-1 RRM23 binding and recognition of target oligonucleotides.
Nucleic Acids Res 45(8):4944-4957 (2017)
Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA
|
| RgGuinier |
2.1 |
nm |
| Dmax |
7.1 |
nm |
| VolumePorod |
32 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
RNA (UUUUUACU) monomer, 1 kDa RNA
|
| Buffer: |
20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7 |
| Experiment: |
SAXS
data collected at SAXS/WAXS, Australian Synchrotron on 2016 May 27
|
TIA-1 RRM23 binding and recognition of target oligonucleotides.
Nucleic Acids Res 45(8):4944-4957 (2017)
Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA
|
| RgGuinier |
2.1 |
nm |
| Dmax |
6.5 |
nm |
| VolumePorod |
26 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Complement C1q subcomponent subunit C hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit B hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit A hexamer, 142 kDa Homo sapiens protein
|
| Buffer: |
50 mM TrisHCl, 145 mM NaCl, 3 mM CaCl2, pH: 7.4 |
| Experiment: |
SAXS
data collected at BM29, ESRF on 2014 Dec 8
|
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade.
Proc Natl Acad Sci U S A 114(5):986-991 (2017)
Mortensen SA, Sander B, Jensen RK, Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
|
|
|
|
|
|
|
|
| Sample: |
Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B Heterodimer dimer, 48 kDa Xenopus laevis protein
Nucleasome Core Particle with Widom 601 DNA - HISTONE H3-H4 Heterodimer dimer, 46 kDa Xenopus laevis protein
Nucleasome Core Particle with Widom 601 DNA - dsDNA monomer, 92 kDa Xenopus laevis DNA
|
| Buffer: |
20 mM Tris-Cl, 0.1 mM EDTA, 0.1 mM DTT, 50% sucrose, 1.2 M NaCl, pH: 7.5 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Apr 14
|
Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the histone core.
Proc Natl Acad Sci U S A 114(2):334-339 (2017)
Chen Y, Tokuda JM, Topping T, Meisburger SP, Pabit SA, Gloss LM, Pollack L
|
|
|
|
|
|
|
|
| Sample: |
Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B Heterodimer dimer, 48 kDa Xenopus laevis protein
Nucleasome Core Particle with Widom 601 DNA - HISTONE H3-H4 Heterodimer dimer, 46 kDa Xenopus laevis protein
Nucleasome Core Particle with Widom 601 DNA - dsDNA monomer, 92 kDa Xenopus laevis DNA
|
| Buffer: |
20 mM Tris-Cl, 0.1 mM EDTA, 0.1 mM DTT, 50% sucrose, 1.9 M NaCl, pH: 7.5 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Apr 14
|
Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the histone core.
Proc Natl Acad Sci U S A 114(2):334-339 (2017)
Chen Y, Tokuda JM, Topping T, Meisburger SP, Pabit SA, Gloss LM, Pollack L
|
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
|
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.
Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
|
| RgGuinier |
2.7 |
nm |
| Dmax |
9.3 |
nm |
| VolumePorod |
110 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris 5 mM NADP+, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Jan 27
|
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.
Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
|
| RgGuinier |
2.6 |
nm |
| Dmax |
8.0 |
nm |
| VolumePorod |
99 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris 5 mM NADP+ 5 mM cyclohexanone, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
|
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.
Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
|
| RgGuinier |
2.5 |
nm |
| Dmax |
7.8 |
nm |
| VolumePorod |
100 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris 5 mM NADP+ 5 mM ε-caprolactone, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
|
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.
Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
|
| RgGuinier |
2.5 |
nm |
| Dmax |
7.5 |
nm |
| VolumePorod |
99 |
nm3 |
|
|
