| MWexperimental | 73 | kDa |
| MWexpected | 76 | kDa |
| VPorod | 105 | nm3 |
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log I(s)
7.91×10-3
7.91×10-4
7.91×10-5
7.91×10-6
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s, nm-1
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Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson.SASDRB5 – ATP-dependent RNA helicase DDX3X (amino acids 1-580) bound to a 15 nucleotide RNA duplex
ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580)15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target)
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Fits and models
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Synchrotron SAXS data from solutions of ATP-dependent RNA helicase DDX3X 1-580) bound to a 15 nucleotide RNA duplex in 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH 8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.4 m and at a wavelength of λ = 1.0322 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 10 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 10/300 column at 16°C. 21 successive 1 second frames were collected through the sample SEC elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
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