| MWI(0) | 72 | kDa |
| MWexpected | 73 | kDa |
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log I(s)
1.39×103
1.39×102
1.39×101
1.39×100
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s, nm-1
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Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.
Gráczer É, Palló A, Oláh J, Szimler T, Konarev PV, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M, FEBS Lett 589(2):240-5 (2015) Europe PMCSASDL57 – Thermus thermophilus 3-isopropylmalate dehydrogenase
3-isopropylmalate dehydrogenase|
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Fits and models
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Synchrotron SAXS
data from solutions of
Thermus thermophilus 3-isopropylmalate dehydrogenase
in
25 mM MOPS/NaOH, pH 7.6
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 2M detector
at a sample-detector distance of 3.1 m and
at a wavelength of λ = 0.124 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 10.00 mg/ml was measured
at 10°C.
20 successive
0.050 second frames were collected.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The OLIGOMER analysis through a concentration series is made available in the full entry zip archive comparing the wild-type and E270A mutant state(s) in the absence and presence of KCl in solution. |
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