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, 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 Journal of Synchrotron Radiation 26(4) (2019)
Stachowski T, Grant T, Snell E
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, 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 Journal of Synchrotron Radiation 26(4) (2019)
Stachowski T, Grant T, Snell E
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 179 nm3

SASDF65 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a) amino acids 1-492

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
BILBOMD model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, Bos taurus protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Small Angle X-ray scattering study of Ric8a
Dhiraj Srivastava
RgGuinier 3.4 nm
Dmax 12.7 nm
VolumePorod 88 nm3

SASDF75 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a) amino acids 1-452

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
PDB model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, Bos taurus protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Small Angle X-ray scattering study of Ric8a
Dhiraj Srivastava
RgGuinier 3.0 nm
Dmax 11.2 nm
VolumePorod 70 nm3

SASDFM5 – Mutant 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, H110A tetramer, at pH 8.5

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, Pseudomonas fluorescens protein
Buffer: 50 mM Tris, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jul 15
Quaternary structure of α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 238 nm3

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