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29 hits found for Nucleic Acids Res

SASDBZ3 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage)/DNA complex (light state)

Aureobox dsDNAAureochrome 1a bZIP-LOV module experimental SAS data
DAMFILT model
Sample: Aureobox dsDNA monomer, synthetic construct DNA
Aureochrome 1a bZIP-LOV module dimer, Phaeodactylum tricornutum protein
Buffer: 50 mM Tris 50 mM boric acid 1 mM EDTA, pH: 8
Experiment: SAXS data collected at BM29, ESRF 2014-Nov-06
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 2016 Jul 8;44(12):5957-70
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 4.5 nm
Dmax 16.7 nm
VolumePorod 97 nm3

SASDB24 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage) module (light state, Tris)

Aureochrome 1a bZIP-LOV module experimental SAS data
Aureochrome 1a bZIP-LOV module Kratky plot
Sample: Aureochrome 1a bZIP-LOV module dimer, Phaeodactylum tricornutum protein
Buffer: 10 mM Tris 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF 2014-Nov-06
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 2016 Jul 8;44(12):5957-70
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 3.9 nm
Dmax 12.5 nm
VolumePorod 121 nm3

SASDBG6 – Ribosome biogenesis protein 15 (Nop15)

Ribosome biogenesis protein 15 experimental SAS data
EOM model
Sample: Ribosome biogenesis protein 15 monomer, Saccharomyces cerevisiae protein
Buffer: 25 mM HEPES, 500 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) 2013-Apr-25
Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. Nucleic Acids Res 2016 Oct 26;
Zhang J, Gonzalez LE, Hall TM
RgGuinier 2.4 nm
Dmax 10.3 nm
VolumePorod 38 nm3

SASDBA7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to Proliferating Cell Nuclear Antigen (PCNA) and DNA

Endonuclease 8-like 1dsDNAProliferating cell nuclear antigen experimental SAS data
DAMMIN model
Sample: Endonuclease 8-like 1 monomer, Homo sapiens protein
dsDNA monomer, DNA
Proliferating cell nuclear antigen monomer, Homo sapiens protein
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) 2016-Jan-20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 2016 Dec 19;
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.4 nm
Dmax 16.4 nm
VolumePorod 113 nm3

SASDBB7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to DNA

Endonuclease 8-like 1dsDNA experimental SAS data
DAMMIN model
Sample: Endonuclease 8-like 1 monomer, Homo sapiens protein
dsDNA monomer, DNA
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) 2016-Jan-20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 2016 Dec 19;
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.3 nm
Dmax 17.5 nm
VolumePorod 92 nm3

SASDBC7 – Human NEI like DNA glycosylase 1 (NEIL1)

Endonuclease 8-like 1 experimental SAS data
GASBOR model
Sample: Endonuclease 8-like 1 monomer, Homo sapiens protein
Buffer: 25mM HEPES 300mM NaCl 1mM DTT 10% Glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS) 2015-Mar-13
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 2016 Dec 19;
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.6 nm
Dmax 15.0 nm
VolumePorod 81 nm3

SASDBD7 – Human Proliferating Cell Nuclear Antigen (PCNA)

Proliferating cell nuclear antigen experimental SAS data
GASBOR model
Sample: Proliferating cell nuclear antigen trimer, Homo sapiens protein
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) 2016-Jan-20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 2016 Dec 19;
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.4 nm
Dmax 9.7 nm
VolumePorod 128 nm3

SASDAN3 – MutS dimer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS dimer, Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at P12, PETRA III 2013-Feb-28
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 2013 Sep;41(17):8166-81
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 4.7 nm
Dmax 15.5 nm
VolumePorod 307 nm3

SASDAQ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS tetramer, Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2011-May-12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 2013 Sep;41(17):8166-81
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 28.0 nm
VolumePorod 700 nm3

SASDBX3 – Aureobox dsDNA

Aureobox dsDNA experimental SAS data
DAMFILT model
Sample: Aureobox dsDNA monomer, synthetic construct DNA
Buffer: 50 mM Tris 50 mM boric acid 1 mM EDTA, pH: 8
Experiment: SAXS data collected at BM29, ESRF 2014-Nov-06
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 2016 Jul 8;44(12):5957-70
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 2.0 nm
Dmax 8.6 nm
VolumePorod 18 nm3

SASDBY3 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage) module (light state-TBE)

Aureochrome 1a bZIP-LOV module experimental SAS data
DAMFILT model
Sample: Aureochrome 1a bZIP-LOV module dimer, Phaeodactylum tricornutum protein
Buffer: 50 mM Tris 50 mM boric acid 1 mM EDTA, pH: 8
Experiment: SAXS data collected at BM29, ESRF 2014-Nov-06
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 2016 Jul 8;44(12):5957-70
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 3.4 nm
Dmax 12.6 nm
VolumePorod 115 nm3

SASDAZ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2011-May-12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 2013 Sep;41(17):8166-81
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.0 nm

SASDA24 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2011-May-12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 2013 Sep;41(17):8166-81
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 27.0 nm

SASDB34 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage) module (dark state, Tris)

Aureochrome 1a bZIP-LOV module experimental SAS data
Aureochrome 1a bZIP-LOV module Kratky plot
Sample: Aureochrome 1a bZIP-LOV module dimer, Phaeodactylum tricornutum protein
Buffer: 10 mM Tris 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF 2014-Nov-06
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 2016 Jul 8;44(12):5957-70
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 117 nm3

SASDBK4 – The 1:1:3:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F short Cascade complex

short-crRNA: CRISPR/Cas Type I-F Cascade componentCas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) experimental SAS data
DAMMIF model
Sample: short-crRNA: CRISPR/Cas Type I-F Cascade component monomer, Shewanella putrefaciens RNA
Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, Shewanella putrefaciens protein
Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) trimer, Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, Shewanella putrefaciens protein
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF 2015-Jun-27
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 2016 May 23;
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 4.1 nm
Dmax 14.2 nm

SASDBL4 – The 1:1:6:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F wild-type Cascade complex

Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)wildtype-crRNA: CRISPR/Cas Type I-F Cascade component experimental SAS data
DAMMIF model
Sample: Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, Shewanella putrefaciens protein
Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) hexamer, Shewanella putrefaciens protein
wildtype-crRNA: CRISPR/Cas Type I-F Cascade component monomer, RNA
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF 2015-Jun-27
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 2016 May 23;
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 5.4 nm
Dmax 18.4 nm

SASDBM4 – The 1:1:9:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F long Cascade complex

Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)long-crRNA: CRISPR/Cas Type I-F Cascade component experimental SAS data
DAMMIF model
Sample: Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, Shewanella putrefaciens protein
Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) nonamer, Shewanella putrefaciens protein
long-crRNA: CRISPR/Cas Type I-F Cascade component monomer, RNA
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF 2016-Jan-30
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 2016 May 23;
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 6.5 nm
Dmax 21.6 nm

SASDAN8 – mLBS1-2 DNA

MHV-68 TR DNA experimental SAS data
CRYSOL model
Sample: MHV-68 TR DNA monomer, unidentified herpesvirus DNA
Buffer: 10 mM TRIS 150 mM NaCl, pH: 7.6
Experiment: SAXS data collected at P12, PETRA III 2013-Apr-27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 2015 Nov 16;43(20):10039-54
...res de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 4.0 nm
Dmax 16.0 nm
VolumePorod 50 nm3

SASDAP8 – kLBS1-2 DNA

kLBS1-2 DNA experimental SAS data
CRYSOL model
Sample: kLBS1-2 DNA monomer, unidentified herpesvirus DNA
Buffer: Tris, pH: 7.6
Experiment: SAXS data collected at BM29, ESRF 2013-Apr-27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 2015 Nov 16;43(20):10039-54
...res de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 4.0 nm
Dmax 16.0 nm
VolumePorod 50 nm3

SASDAQ8 – kLANA mutant dimer-tetramer mixture

ORF73 tetramerORF73 dimer experimental SAS data
OLIGOMER model
Sample: ORF73 tetramer tetramer, Human herpesvirus 8 protein
ORF73 dimer dimer, Human herpesvirus 8 protein
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF 2014-Jun-21
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 2015 Nov 16;43(20):10039-54
...res de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 2.4 nm
Dmax 9.5 nm
VolumePorod 50 nm3

SASDAR8 – mLANA 124-316 mLBS1-2 8:1 complex

MHV-68 TR DNALatency-associated nuclear antigen experimental SAS data
CRYSOL model
Sample: MHV-68 TR DNA monomer, unidentified herpesvirus DNA
Latency-associated nuclear antigen octamer, Murid herpesvirus 4 protein
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at P12, PETRA III 2013-Apr-27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 2015 Nov 16;43(20):10039-54
...res de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 5.8 nm
Dmax 20.0 nm
VolumePorod 475 nm3

SASDAS8 – kLANA 1008-1150 -- kLBS1-2 complex 8:2 (partially dissociated)

kLBS1-2 DNAORF73 tetramerORF73 octamerkLBS1-2 DNA two monomers experimental SAS data
OLIGOMER model
Sample: kLBS1-2 DNA monomer, unidentified herpesvirus DNA
ORF73 tetramer tetramer, Human herpesvirus 8 protein
ORF73 octamer octamer, Human herpesvirus 8 protein
kLBS1-2 DNA two monomers dimer, unidentified herpesvirus RNA
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at P12, PETRA III 2013-Apr-27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 2015 Nov 16;43(20):10039-54
...res de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 4.8 nm
Dmax 16.0 nm
VolumePorod 250 nm3

SASDAG5 – RNA shaperone Hfq

RNA chaperone Hfq experimental SAS data
DAMMIN model
Sample: RNA chaperone Hfq hexamer, Escherichia coli protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2008-May-02
Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. Nucleic Acids Res 2011 Jun;39(11):4900-15
Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K
RgGuinier 3.2 nm
Dmax 11.2 nm
VolumePorod 110 nm3

SASDAH5 – Complex of Hfq with DsrA

RNA chaperone HfqRNA DsrA experimental SAS data
SASREF model
Sample: RNA chaperone Hfq hexamer, Escherichia coli protein
RNA DsrA monomer, RNA
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2010-Nov-16
Structural flexibility of RNA as molecular basis for Hfq chaperone function. Nucleic Acids Res 2012 Sep;40(16):8072-84
Ribeiro Ede A Jr, Beich-Frandsen M, Konarev PV, Shang W, Vecerek B, Kontaxis G, Hämmerle H, Peterlik H, Svergun DI, Bläsi U, Djinović-Carugo K
RgGuinier 4.3 nm
Dmax 14.5 nm
VolumePorod 210 nm3

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2011-May-12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 2013 Sep;41(17):8166-81
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.5 nm
Dmax 29.0 nm
VolumePorod 750 nm3

SASDAM8 – MHV-68 LANA

Latency-associated nuclear antigen experimental SAS data
MHV-68 LANA Rg histogram
Sample: Latency-associated nuclear antigen tetramer, Murid herpesvirus 4 protein
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at P12, PETRA III 2013-Apr-27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 2015 Nov 16;43(20):10039-54
...res de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 4.2 nm
Dmax 16.0 nm
VolumePorod 117 nm3

SASDAY3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at X33, DORIS III 2011-May-12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 2013 Sep;41(17):8166-81
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.3 nm
Dmax 29.0 nm
VolumePorod 720 nm3

SASDAV5 – apo XMRV RT

apo XMRV RT experimental SAS data
CRYSOL model
Sample: apo XMRV RT monomer, Escherichia coli protein
Buffer: 10 mM HEPES 100 mM KCl 5% Glycerol, pH: 6.5
Experiment: SAXS data collected at X33, DORIS III 2011-Dec-08
Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid. Nucleic Acids Res 2013 Apr 1;41(6):3874-87
Nowak E, Potrzebowski W, Konarev PV, Rausch JW, Bona MK, Svergun DI, Bujnicki JM, Le Grice SF, Nowotny M
RgGuinier 4.0 nm
Dmax 13.5 nm
VolumePorod 160 nm3

SASDAW5 – XMRV RT + DNA/RNA hybrid

apo XMRV RTRNA_DNA hybrid substrate experimental SAS data
CRYSOL model
Sample: apo XMRV RT monomer, Escherichia coli protein
RNA_DNA hybrid substrate monomer, other
Buffer: 10 mM HEPES 100 mM KCl 5% Glycerol, pH: 6.5
Experiment: SAXS data collected at X33, DORIS III 2011-Dec-08
Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid. Nucleic Acids Res 2013 Apr 1;41(6):3874-87
Nowak E, Potrzebowski W, Konarev PV, Rausch JW, Bona MK, Svergun DI, Bujnicki JM, Le Grice SF, Nowotny M
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 155 nm3