Browse by DISSEMINATION: Published

SASDBL6 – Truncated construct of human p23 (1-117)

Prostaglandin E synthase 3 (1-117) experimental SAS data
Prostaglandin E synthase 3 (1-117) Kratky plot
Sample: Prostaglandin E synthase 3 (1-117) monomer, 14 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 29 nm3

SASDC85 – Leishmania braziliensis p23B

Leishmania braziliensis p23 isoform B experimental SAS data
DAMFILT model
Sample: Leishmania braziliensis p23 isoform B monomer, 23 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC
RgGuinier 3.0 nm
Dmax 13.0 nm

SASDCV5 – Leishmania braziliensis p23A

Uncharacterized protein experimental SAS data
DAMFILT model
Sample: Uncharacterized protein monomer, 22 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC
RgGuinier 3.3 nm
Dmax 13.0 nm

SASDLP5 – Complex of the josephin domain of ataxin-3 with ubiquitin

Josephin domain of ataxin-3Polyubiquitin-B experimental SAS data
DAMMIF model
Sample: Josephin domain of ataxin-3 monomer, 21 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 2 mM DTT, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 7
Allosteric regulation of deubiquitylase activity through ubiquitination. Front Mol Biosci 2:2 (2015)
Faggiano S, Menon RP, Kelly GP, Todi SV, Scaglione KM, Konarev PV, Svergun DI, Paulson HL, Pastore A
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 45 nm3

SASDLH3 – Truncated Thermoplasma E2 catalytic core

Regulatory protein E2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Regulatory protein E2 trimer, 73 kDa Human papillomavirus type … protein
Buffer: 50 mM Tris ⁄ HCl, pH 8.8, 100 mM NaCl, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 27
Why are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complex Biochemical Journal 463(3):405-412 (2014)
Marrott N, Marshall J, Svergun D, Crennell S, Hough D, van den Elsen J, Danson M
RgGuinier 3.1 nm
Dmax 11.0 nm
VolumePorod 149 nm3

SASDAZ5 – NetrinVIV

Netrin-1 experimental SAS data
DAMMIN model
Sample: Netrin-1 monomer, 49 kDa Homo sapiens protein
Buffer: 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 26
The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83(4):839-849 (2014)
Finci LI, Krüger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R
RgGuinier 3.9 nm
Dmax 13.5 nm
VolumePorod 100 nm3

SASDA26 – DCC56

Deleted in Colorectal Cancer (FN5 & FN6) experimental SAS data
DAMMIN model
Sample: Deleted in Colorectal Cancer (FN5 & FN6) monomer, 26 kDa Homo sapiens protein
Buffer: 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 26
The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83(4):839-849 (2014)
Finci LI, Krüger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R
RgGuinier 3.2 nm
Dmax 11.0 nm
VolumePorod 38 nm3

SASDA76 – NetrinVIV DCC56 complex

Netrin-1Deleted in Colorectal Cancer (FN5 & FN6) experimental SAS data
Netrin-1 Deleted in Colorectal Cancer (FN5 & FN6) Kratky plot
Sample: Netrin-1 monomer, 49 kDa Homo sapiens protein
Deleted in Colorectal Cancer (FN5 & FN6) monomer, 26 kDa Homo sapiens protein
Buffer: 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83(4):839-849 (2014)
Finci LI, Krüger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R
RgGuinier 5.1 nm
Dmax 17.0 nm
VolumePorod 120 nm3

SASDA86 – NetrinVIV DCC56(M933R) complex

Netrin-1Deleted in Colorectal Cancer (FN5 & FN6) M933R mutant experimental SAS data
Netrin-1 Deleted in Colorectal Cancer (FN5 & FN6) M933R mutant Kratky plot
Sample: Netrin-1 monomer, 49 kDa Homo sapiens protein
Deleted in Colorectal Cancer (FN5 & FN6) M933R mutant monomer, 26 kDa Homo sapiens protein
Buffer: 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 26
The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83(4):839-849 (2014)
Finci LI, Krüger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R
RgGuinier 4.0 nm
Dmax 14.0 nm
VolumePorod 95 nm3

SASDAL5 – Clostridium difficile bacteriophage 27 endolysin dimer, CD27L

Clostridium difficile bacteriophage 27 endolysin experimental SAS data
NONE model
Sample: Clostridium difficile bacteriophage 27 endolysin dimer, 64 kDa Clostridioides difficile protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
The CD27L and CTP1L endolysins targeting Clostridia contain a built-in trigger and release factor. PLoS Pathog 10(7):e1004228 (2014)
Dunne M, Mertens HD, Garefalaki V, Jeffries CM, Thompson A, Lemke EA, Svergun DI, Mayer MJ, Narbad A, Meijers R
RgGuinier 3.3 nm
Dmax 10.6 nm
VolumePorod 72 nm3