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6 hits found for Soni

SASDK24 – Signal recognition particle SRP9/14 heterodimer from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14 experimental SAS data
DAMMIN model
Sample: Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein
Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Feb 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 2.1 nm
Dmax 7.2 nm
VolumePorod 47 nm3

SASDK34 – Full length SRP Alu RNA from Plasmodium falciparum

Full-length SRP Alu RNA experimental SAS data
DAMMIN model
Sample: Full-length SRP Alu RNA monomer, 38 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.3 nm
Dmax 11.8 nm
VolumePorod 63 nm3

SASDK44 – The 5' domain of SRP Alu RNA from Plasmodium falciparum

SRP Alu RNA 5' domain experimental SAS data
DAMMIN model
Sample: SRP Alu RNA 5' domain monomer, 24 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.3 nm
Dmax 11.5 nm
VolumePorod 38 nm3

SASDK54 – Signal recognition particle SRP9/14 heterodimer in complex with full length SRP Alu RNA from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14Full-length SRP Alu RNA experimental SAS data
MONSA model
Sample: Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein
Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein
Full-length SRP Alu RNA monomer, 38 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.5 nm
Dmax 12.0 nm
VolumePorod 120 nm3

SASDK64 – Signal recognition particle SRP9/14 heterodimer in complex with the 5' domain of SRP Alu RNA from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14SRP Alu RNA 5' domain experimental SAS data
MONSA model
Sample: Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein
Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein
SRP Alu RNA 5' domain monomer, 24 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.2 nm
Dmax 11.9 nm
VolumePorod 77 nm3

SASDHJ8 – ACT domain of the Mycobacterium tuberculosis Rel protein

ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) experimental SAS data
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) Kratky plot
Sample: ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) dimer, 20 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 350 mM NaCl, 5% glycerol, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar, Nanyang Technological University on 2018 Jun 7
Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein. FEBS J (2020)
Shin J, Singal B, Manimekalai MSS, Chen MW, Ragunathan P, GrĂ¼ber G
RgGuinier 1.9 nm
Dmax 6.1 nm
VolumePorod 29 nm3