Browse by MODEL: No model

SASDGR2 – Thymine dioxygenase J-containing DNA binding domain (JDBD)

J-DNA binding domain experimental SAS data
J-DNA binding domain Kratky plot
Sample: J-DNA binding domain monomer, 21 kDa Leishmania tarentolae protein
Buffer: 20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 4
The domain architecture of protozoan protein J-DNA-binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity. J Biol Chem (2019)
Adamopoulos A, Heidebrecht T, Roosendaal J, Touw WG, Phan IQ, Beijnen J, Perrakis A
RgGuinier 2.2 nm
Dmax 7.1 nm
VolumePorod 38 nm3

SASDGS2 – J-23-DNA

J-DNA (23mer) experimental SAS data
J-DNA (23mer) Kratky plot
Sample: J-DNA (23mer) monomer, 14 kDa DNA
Buffer: 20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 21
The domain architecture of protozoan protein J-DNA-binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity. J Biol Chem (2019)
Adamopoulos A, Heidebrecht T, Roosendaal J, Touw WG, Phan IQ, Beijnen J, Perrakis A
RgGuinier 2.3 nm
Dmax 7.3 nm
VolumePorod 20 nm3

SASDGT2 – Thymine dioxygenase J-containing DNA binding domain in complex with J-23-DNA (JDBD:J-23-DNA)

J-DNA binding domainJ-DNA (23mer) experimental SAS data
J-DNA binding domain J-DNA (23mer) Kratky plot
Sample: J-DNA binding domain monomer, 21 kDa Leishmania tarentolae protein
J-DNA (23mer) monomer, 14 kDa DNA
Buffer: 20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 21
The domain architecture of protozoan protein J-DNA-binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity. J Biol Chem (2019)
Adamopoulos A, Heidebrecht T, Roosendaal J, Touw WG, Phan IQ, Beijnen J, Perrakis A
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 43 nm3

SASDGU2 – Thymine dioxygenase full length J-DNA binding protein in complex with J-23-DNA (JBP1:J-23-DNA)

Thymine dioxygenase JBP1J-DNA (23mer) experimental SAS data
Thymine dioxygenase JBP1 J-DNA (23mer) Kratky plot
Sample: Thymine dioxygenase JBP1 monomer, 93 kDa Leishmania tarentolae protein
J-DNA (23mer) monomer, 14 kDa DNA
Buffer: 20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 21
The domain architecture of protozoan protein J-DNA-binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity. J Biol Chem (2019)
Adamopoulos A, Heidebrecht T, Roosendaal J, Touw WG, Phan IQ, Beijnen J, Perrakis A
RgGuinier 4.1 nm
Dmax 14.1 nm
VolumePorod 148 nm3

SASDFD2 – wild-type human Latent Transforming Growth Factor beta 1 (LTGFB-1)

Human Latent Transforming Growth Factor beta 1 experimental SAS data
Human Latent Transforming Growth Factor beta 1 Kratky plot
Sample: Human Latent Transforming Growth Factor beta 1 dimer, 86 kDa Homo sapiens protein
Buffer: phosphate buffered saline 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 4
Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses. J Synchrotron Radiat 26(Pt 4):967-979 (2019)
Stachowski T, Grant TD, Snell EH
RgGuinier 3.8 nm
Dmax 17.5 nm
VolumePorod 200 nm3

SASDFE2 – wild-type human Latency Associated Peptide (LAP)

Latency Associated Peptide experimental SAS data
Latency Associated Peptide Kratky plot
Sample: Latency Associated Peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 4
Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses. J Synchrotron Radiat 26(Pt 4):967-979 (2019)
Stachowski T, Grant TD, Snell EH
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 179 nm3

SASDFB4 – Insulin glargine (Lantus ®), oligomeric mixture

Insulin glargine (Lantus ®) experimental SAS data
Insulin glargine (Lantus ®) Kratky plot
Sample: Insulin glargine (Lantus ®) hexamer, 36 kDa protein
Buffer: Lantus Formulation (30 µg Zinc cloride, 2.7 mg m-Cresol, 20 mg glycerol 85%), pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 May 23
The quaternary structure of insulin glargine and glulisine under formulation conditions. Biophys Chem 253:106226 (2019)
Nagel N, Graewert MA, Gao M, Heyse W, Jeffries CM, Svergun D, Berchtold H
RgGuinier 1.8 nm
Dmax 5.3 nm

SASDDY9 – Protein translocase subunit SecA (full length, amino acids 1-901)

Protein translocase subunit SecA experimental SAS data
Protein translocase subunit SecA Kratky plot
Sample: Protein translocase subunit SecA dimer, 204 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, 1mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 18
The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife 8 (2019)
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D
RgGuinier 4.2 nm
Dmax 14.9 nm
VolumePorod 424 nm3

SASDDZ9 – Protein translocase subunit SecA (amino acids 1-880)

Protein translocase subunit SecA experimental SAS data
Protein translocase subunit SecA Kratky plot
Sample: Protein translocase subunit SecA dimer, 199 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, 1mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 18
The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife 8 (2019)
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D
RgGuinier 4.2 nm
Dmax 14.8 nm
VolumePorod 380 nm3

SASDE22 – Protein translocase subunit SecA (amino acids 1-832)

Protein translocase subunit SecA experimental SAS data
Protein translocase subunit SecA Kratky plot
Sample: Protein translocase subunit SecA dimer, 189 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, 1mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 18
The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity. Elife 8 (2019)
Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D
RgGuinier 4.5 nm
Dmax 15.7 nm
VolumePorod 398 nm3