| 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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