Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
Gruszka DT,
Whelan F,
Farrance OE,
Fung HK,
Paci E,
Jeffries CM,
Svergun DI,
Baldock C,
Baumann CG,
Brockwell DJ,
Potts JR,
Clarke J
Nat Commun
6:7271
(2015 Jun 1)
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| Sample: |
Surface protein G monomer, 24 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Nov 12
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| RgGuinier |
4.7 |
nm |
| Dmax |
19.0 |
nm |
| VolumePorod |
29 |
nm3 |
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| Sample: |
Surface protein G monomer, 39 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Nov 12
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| RgGuinier |
7.7 |
nm |
| Dmax |
30.5 |
nm |
| VolumePorod |
49 |
nm3 |
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| Sample: |
Surface protein G monomer, 53 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Nov 12
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| RgGuinier |
9.7 |
nm |
| Dmax |
38.5 |
nm |
| VolumePorod |
58 |
nm3 |
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| Sample: |
Surface protein G monomer, 67 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Nov 12
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| RgGuinier |
12.0 |
nm |
| Dmax |
48.0 |
nm |
| VolumePorod |
87 |
nm3 |
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| Sample: |
Surface protein G monomer, 81 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Nov 12
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|
| RgGuinier |
14.1 |
nm |
| Dmax |
57.0 |
nm |
| VolumePorod |
89 |
nm3 |
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| Sample: |
Surface protein G monomer, 95 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Nov 12
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| RgGuinier |
15.9 |
nm |
| Dmax |
63.0 |
nm |
| VolumePorod |
122 |
nm3 |
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