Browse by ORGANISM: other species

SASDCW9 – Bacteriophage phi-X174 - ~245s after mixing with LPS

Bacteriophage phi-X174 experimental SAS data
Bacteriophage phi-X174 Kratky plot
Sample: Bacteriophage phi-X174 monomer, 0 kDa protein
Buffer: 0.15 mg/mL LPS, 0.06 M NH4Cl2, 0.09 M NaCl, 0.1 M KCl, 1 mM MgS04, 1 mM CaCl2, 0.1 M Tris-HCl, pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 25
Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A 114(52):13708-13713 (2017)
Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG
RgGuinier 12.9 nm

SASDCX9 – Bacteriophage phi-X174 - ~545s after mixing with LPS

Bacteriophage phi-X174 experimental SAS data
Bacteriophage phi-X174 Kratky plot
Sample: Bacteriophage phi-X174 monomer, 0 kDa protein
Buffer: 0.15 mg/mL LPS, 0.06 M NH4Cl2, 0.09 M NaCl, 0.1 M KCl, 1 mM MgS04, 1 mM CaCl2, 0.1 M Tris-HCl, pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 25
Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A 114(52):13708-13713 (2017)
Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG
RgGuinier 12.9 nm

SASDBY4 – Pentameric Nucleoplasmin-histone H2A/H2B complex

Nucleoplasmin core + A2Histone H2A (ΔAla127)Histone H2B 1.1 (Ser33Thr) experimental SAS data
DAMFILT model
Sample: Nucleoplasmin core + A2 pentamer, 81 kDa Xenopus laevis protein
Histone H2A (ΔAla127) pentamer, 69 kDa Xenopus laevis protein
Histone H2B 1.1 (Ser33Thr) pentamer, 67 kDa Xenopus laevis protein
Buffer: 20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2016 Jan 7
Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. Nat Commun 8(1):2215 (2017)
Warren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D
RgGuinier 4.4 nm
Dmax 14.0 nm
VolumePorod 402 nm3

SASDCB7 – Streptococcus pneumoniae phosphodiesterase Pde2

DHH subfamily 1 protein experimental SAS data
DHH subfamily 1 protein Kratky plot
Sample: DHH subfamily 1 protein dimer, 70 kDa Streptococcus pneumoniae serotype … protein
Buffer: 20mM Tris, 200 mM NaCl, 5%(v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 23
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.7 nm
Dmax 7.7 nm
VolumePorod 87 nm3

SASDCC7 – Thermotoga martitima phosphodiesterase TM1595 D80N D154N (inactive mutant)

T.maritima PDE experimental SAS data
T.maritima PDE Kratky plot
Sample: T.maritima PDE dimer, 76 kDa Thermotoga maritima protein
Buffer: 25mM Tris 500mM NaCl 3% (v/v) glycerol 2mM MgCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jun 17
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 115 nm3

SASDCD7 – Thermotoga maritima phosphodiesterase TM1595 (wildtype, TmPde)

Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) dimer, 76 kDa Thermotoga maritima protein
Buffer: 20mM Tris, 200 mM NaCl, 5%(v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 23
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.7 nm
Dmax 7.8 nm
VolumePorod 106 nm3

SASDB89 – Telomeric DNA duplex

telomere DNA duplex experimental SAS data
MONSA model
Sample: Telomere DNA duplex monomer, 11 kDa DNA
Buffer: 20 mM Tris-HCl, 50 mM LiCl, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2016 May 3
Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it. Nucleic Acids Res 45(21):12170-12180 (2017)
Necasová I, Janoušková E, Klumpler T, Hofr C
RgGuinier 1.6 nm
Dmax 5.7 nm
VolumePorod 12 nm3

SASDCK9 – Catalytic domain (AC) of B. Pertussis Adenylate Cyclase Toxin (CyaA)

Bifunctional hemolysin/adenylate cyclase experimental SAS data
ALLOSMOD model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 39 kDa Bordetella pertussis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 4 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Jun 19
Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis. PLoS Biol 15(12):e2004486 (2017)
O'Brien DP, Durand D, Voegele A, Hourdel V, Davi M, Chamot-Rooke J, Vachette P, Brier S, Ladant D, Chenal A
RgGuinier 2.6 nm
Dmax 9.1 nm
VolumePorod 60 nm3

SASDBJ7 – Pomacea maculata perivitellin 1

Pomacea maculata perivitellin 1 experimental SAS data
DAMMIF model
Sample: Pomacea maculata perivitellin 1 dodecamer, 278 kDa Pomacea maculata protein
Buffer: 100 mM Phosphate Buffer, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 Mar 26
Convergent evolution of plant and animal embryo defences by hyperstable non-digestible storage proteins. Sci Rep 7(1):15848 (2017)
Pasquevich MY, Dreon MS, Qiu JW, Mu H, Heras H
RgGuinier 4.2 nm
Dmax 14.3 nm
VolumePorod 537 nm3

SASDCN5 – Vaccinia virus DNA polymerase

DNA polymerase E9 experimental SAS data
PYMOL model
Sample: DNA polymerase E9 monomer, 117 kDa Vaccinia virus protein
Buffer: 20 mM Tris HCl, 100 mM NaCl, 4 mM DTT, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 27
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding. Nat Commun 8(1):1455 (2017)
Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F
RgGuinier 3.9 nm
Dmax 12.0 nm
VolumePorod 202 nm3