| MWexperimental | 101 | kDa |
| MWexpected | 116 | kDa |
| VPorod | 160 | nm3 |
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log I(s)
4.39×10-2
4.39×10-3
4.39×10-4
4.39×10-5
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s, nm-1
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Structural and functional investigation of tRNA guanine transglycosylase
Katharina Sievers, University of Göttingen Dissertation - (2023) URLSASDRC8 – Human tRNA guanine transglycosylase bound to aspartate transfer RNA (tRNA-Asp)
Queuine tRNA-ribosyltransferase catalytic subunit 1Queuine tRNA-ribosyltransferase accessory subunit 2
transfer RNA (Aspartate)
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of tRNA guanine transglycosylase bound to aspartate transfer RNA in 20 mM HEPES, 100 mM NaCl, 3% (w/v) glycerol, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 75.00 μl sample at 4.5 mg/ml was injected at a 0.70 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 2160 successive 1 second frames were collected through the SEC elution. 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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