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5 hits found for Sah-Teli

SASDJS5 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-monomer

Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data
DAMMIN model
Sample: Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial monomer, 70 kDa Saccharomyces cerevisiae protein
Buffer: 40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 1
Expression and analysis of the SAM-dependent RNA methyltransferase Rsm22 from Saccharomyces cerevisiae Acta Crystallographica Section D Structural Biology 77(6) (2021)
...Sah-Teli S, Venkatesan R, Koski M, Autio K, Hiltunen J, Kastaniotis A
RgGuinier 3.8 nm
Dmax 13.9 nm
VolumePorod 160 nm3

SASDJT5 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-dimer

dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data
DAMMIN model
Sample: dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial dimer, 141 kDa Saccharomyces cerevisiae protein
Buffer: 40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 1
Expression and analysis of the SAM-dependent RNA methyltransferase Rsm22 from Saccharomyces cerevisiae Acta Crystallographica Section D Structural Biology 77(6) (2021)
...Sah-Teli S, Venkatesan R, Koski M, Autio K, Hiltunen J, Kastaniotis A
RgGuinier 5.0 nm
Dmax 18.2 nm
VolumePorod 516 nm3

SASDKS8 – Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme subunit alpha (anEcTFE-alpha)

Fatty acid oxidation complex subunit alpha experimental SAS data
DAMMIF model
Sample: Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli (strain … protein
Buffer: 50 mM Tris, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 9
Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial β-oxidation trifunctional enzymes. Structure (2023)
Sah-Teli SK, Pinkas M, Hynönen MJ, Butcher SJ, Wierenga RK, Novacek J, Venkatesan R
RgGuinier 3.3 nm
Dmax 11.2 nm
VolumePorod 145 nm3

SASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaFatty acid oxidation complex subunit alpha3-ketoacyl-CoA thiolase FadA (beta subunit) experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
3-ketoacyl-CoA thiolase FadA (beta subunit) dimer, 82 kDa Escherichia coli protein
Buffer: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 30
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 406 nm3

SASDEM9 – anEcTFE: Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic 3-ketoacyl-CoA thiolase FadI beta subunitanaerobic 3-ketoacyl-CoA thiolase FadI beta subunit experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli (strain … protein
anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
Buffer: 50 mM Tris, 500 mM NaCl, 5% glycerol, 0.05% C12E9 (1-O-(n-Dodecyl)-nonaethyleneglycol), 2.5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 22
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 6.2 nm
Dmax 19.6 nm
VolumePorod 856 nm3