| MWI(0) | 72 | kDa |
| MWexpected | 73 | kDa |
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log I(s)
1.46×104
1.46×103
1.46×102
1.46×101
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s, nm-1
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Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.
Gráczer É, Szimler T, Garamszegi A, Konarev PV, Lábas A, Oláh J, Palló A, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M, Biochemistry 55(3):560-74 (2016) Europe PMCSASDL67 – Mutation of the Active Site Residues of 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
Mutation of the Active Site Residues 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 4.52 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 is made available in the full entry zip archive comparing for the D217A, D245A, K185A, N102A, and Y139A mutant state(s) in solution. |
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