| MWexperimental | 191 | kDa |
| MWexpected | 180 | kDa |
| VPorod | 262 | nm3 |
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log I(s)
9.94×102
9.94×101
9.94×100
9.94×10-1
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s, nm-1
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The Active Conformation of Glutamate Synthase and its Binding to Ferredoxin
van den Heuvel R, Svergun D, Petoukhov M Coda A, Curti B, Ravasio S, Vanoni M, Mattevi A, Journal of Molecular Biology 330(1):113-128 (2003) DOISASDLN7 – 1:1 complex of Ferredoxin-dependent glutamate synthase 2 (FdGlts) with ferredoxin
Ferredoxin-dependent glutamate synthase 2Ferredoxin-1
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Fits and models
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Synchrotron SAXS data from the 1:1 complex formed between ferredoxin-dependent glutamate synthase 2 (FdGlts) and ferredoxin in Hepes– KOH buffer, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III storage ring (DESY, Hamburg, Germany) using a 1D Gas detector detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 3 and 17 mg/ml were measured . The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
Experimental temperature: UNKNOWN. X-ray exposure time: UNKNOWN. Specific buffer composition: UNKNOWN.
Tags:
X33
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