How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
        
            
                  
                    
                        Mias-Lucquin D,
                    
                  
                    
                        
 Dos Santos Morais R,
                    
                  
                    
                         Chéron A,
                    
                  
                    
                         Lagarrigue M,
                    
                  
                    
                         Winder SJ,
                    
                  
                    
                         Chenuel T,
                    
                  
                    
                         Pérez J,
                    
                  
                    
                         Appavou MS,
                    
                  
                    
                         Martel A,
                    
                  
                    
                         Alviset G,
                    
                  
                    
                         Le Rumeur E,
                    
                  
                    
                         Combet S,
                    
                  
                    
                         Hubert JF,
                    
                  
                    
                         Delalande O
                    
                  
                
                
J Struct Biol
                :107411
                (2019 Nov 2)
                
            
        
    
    
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		| Sample: | Human dystrophin central domain R8-15 fragment monomer, 100 kDa  protein 
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		| Buffer: | NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5 |  
		| Experiment: | SAXS  
			data collected at SWING, SOLEIL on 2015 Sep 23 |  | 
	
		
			| RgGuinier | 10.1 | nm |  
			| Dmax | 36.0 | nm |  |  | 
    
        
    
    
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		| Sample: | Human dystrophin central domain R11-19 fragment monomer, 117 kDa  protein 
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		| Buffer: | NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5 |  
		| Experiment: | SAXS  
			data collected at SWING, SOLEIL on 2017 May 11 |  | 
	
		
			| RgGuinier | 8.8 | nm |  
			| Dmax | 37.5 | nm |  
			| VolumePorod | 513 | nm3 |  |  | 
    
        
    
    
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		| Sample: | Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein 
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		| Buffer: | 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1 |  
		| Experiment: | SANS  
			data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1 |  | 
	
		
			| RgGuinier | 6.2 | nm |  
			| Dmax | 27.4 | nm |  
			| VolumePorod | 146 | nm3 |  |  | 
    
        
    
    
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		| Sample: | Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein 
 |  
		| Buffer: | 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1 |  
		| Experiment: | SANS  
			data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1 |  | 
	
		
			| RgGuinier | 6.2 | nm |  
			| Dmax | 28.1 | nm |  
			| VolumePorod | 144 | nm3 |  |  | 
    
        
    
    
        | 
	
		|  |  
		|  |   | 
	
		| Sample: | Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein 
 |  
		| Buffer: | 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1 |  
		| Experiment: | SANS  
			data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1 |  | 
	
		
			| RgGuinier | 8.1 | nm |  
			| Dmax | 29.6 | nm |  
			| VolumePorod | 231 | nm3 |  |  |