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23 hits found for White

SASDH62 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 7
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
...White MA, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 123 nm3

SASDH72 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 8
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
...White MA, Cheng X
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 151 nm3

SASDH82 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 11
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
...White MA, Cheng X
RgGuinier 3.6 nm
Dmax 11.4 nm
VolumePorod 145 nm3

SASDDP3 – N-propargyl glycine-Inactivated Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) collected by SEC-SAXS

Bifunctional protein PutA experimental SAS data
PDB model
Sample: Bifunctional protein PutA dimer, 215 kDa Bradyrhizobium diazoefficiens (strain … protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM TCEP, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Jul 16
Redox Modulation of Oligomeric State in Proline Utilization A. Biophys J 114(12):2833-2843 (2018)
...White TA, Becker DF, Tanner JJ
RgGuinier 4.6 nm
Dmax 14.4 nm
VolumePorod 324 nm3

SASDDQ3 – Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) collected by SEC-SAXS

Bifunctional protein PutA experimental SAS data
PDB model
Sample: Bifunctional protein PutA tetramer, 430 kDa Bradyrhizobium diazoefficiens (strain … protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM TCEP, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Jul 16
Redox Modulation of Oligomeric State in Proline Utilization A. Biophys J 114(12):2833-2843 (2018)
...White TA, Becker DF, Tanner JJ
RgGuinier 5.2 nm
Dmax 14.2 nm
VolumePorod 582 nm3

SASDD95 – Neurexin 1a L5L6

Neurexin 1a L5L6 experimental SAS data
Neurexin 1a L5L6 Rg histogram
Sample: Neurexin 1a L5L6 monomer, 44 kDa protein
Buffer: 20 mM HEPES pH 8, 150 mM NaCl, 0.5mM CaCl2, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2016 Sep 6
Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer. J Mol Biol 430(21):4325-4343 (2018)
...White MA, Ren G, Rudenko G
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 69 nm3

SASDDA5 – Neurexin 1a L5L6 with ss6 insert

Neurexin 1a L5L6 with ss6 insert experimental SAS data
Neurexin 1a L5L6 with ss6 insert Rg histogram
Sample: Neurexin 1a L5L6 with ss6 insert monomer, 45 kDa Homo sapiens protein
Buffer: 20 mM HEPES pH 8, 150 mM NaCl, 0.5mM CaCl2, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2016 Sep 26
Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer. J Mol Biol 430(21):4325-4343 (2018)
...White MA, Ren G, Rudenko G
RgGuinier 3.2 nm
Dmax 12.4 nm
VolumePorod 70 nm3

SASDCQ6 – Rap guanine nucleotide exchange factor 3 (isoform3) - apo form

Rap guanine nucleotide exchange factor 3 experimental SAS data
SWISSMODEL model
Sample: Rap guanine nucleotide exchange factor 3 monomer, 100 kDa Homo sapiens protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2012 Sep 7
Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology. Cells 9(1) (2019)
White MA, Tsalkova T, Mei FC, Cheng X
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 180 nm3

SASDCR6 – Rap guanine nucleotide exchange factor 3 (isoform3) - binary form with cAMP

Rap guanine nucleotide exchange factor 3 (dimer) experimental SAS data
CORAL model
Sample: Rap guanine nucleotide exchange factor 3 (dimer) dimer, 200 kDa Homo sapiens protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2012 Jan 30
Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology. Cells 9(1) (2019)
White MA, Tsalkova T, Mei FC, Cheng X
RgGuinier 5.3 nm
Dmax 15.7 nm
VolumePorod 415 nm3

SASDCS6 – Rap guanine nucleotide exchange factor 3 (isoform3) bound to RAS related protein 1b - with cAMP

Rap guanine nucleotide exchange factor 3RAS related protein 1b experimental SAS data
SWISSMODEL model
Sample: Rap guanine nucleotide exchange factor 3 monomer, 100 kDa Homo sapiens protein
RAS related protein 1b monomer, 18 kDa Mus musculus protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2013 Apr 1
Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology. Cells 9(1) (2019)
White MA, Tsalkova T, Mei FC, Cheng X
RgGuinier 4.1 nm
Dmax 14.2 nm
VolumePorod 207 nm3

SASDDV8 – Boiled chicken egg albumen

Ovalbumin experimental SAS data
Ovalbumin Kratky plot
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDW8 – Chinese century egg albumen (pidan) made from quail egg

Ovalbumin (common quail) experimental SAS data
Ovalbumin (common quail) Kratky plot
Sample: Ovalbumin (common quail) monomer, 42 kDa Coturnix coturnix protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDX8 – Raw chicken egg albumen

Ovalbumin experimental SAS data
Ovalbumin Kratky plot
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDY8 – Chicken ovalbumin gel at high pH

Ovalbumin experimental SAS data
DAMMIF model
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: 0.16 M NaOH, pH: 13.2
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 Feb 21
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDD29 – Low load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
...White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.5 nm
VolumePorod 212 nm3

SASDD39 – Medium load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
...White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.7 nm
VolumePorod 229 nm3

SASDD49 – High load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
...White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.7 nm
VolumePorod 238 nm3

SASDD59 – Low load concentration of alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, 1 mM NAD, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
...White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.7 nm
VolumePorod 277 nm3

SASDD69 – Medium load concentration of alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, 1 mM NAD, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
...White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.8 nm
VolumePorod 275 nm3

SASDD79 – High load concentration of alpha-aminoadipic semialdehyde dehydrogenase ALDH7A1 with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, 1 mM NAD, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
...White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.8 nm
VolumePorod 277 nm3

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 (strain … 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)
...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 (strain … 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)
...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 (strain … 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)
...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