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6 hits found for Beta-amylase 2, chloroplastic

SASDUZ9 – BAM2 in 100 mM KCl (0.5 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.9 nm
Dmax 15.0 nm
VolumePorod 234 nm3

SASDV22 – BAM2 in 100 mM KCl (1 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.7 nm
Dmax 15.1 nm
VolumePorod 218 nm3

SASDV32 – BAM2 in 100 mM KCl (2 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.7 nm
Dmax 15.0 nm
VolumePorod 220 nm3

SASDGY4Beta-amylase 2, chloroplastic (AtBAM2)

Beta-amylase 2, chloroplastic experimental SAS data
YASARA model
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
Solution structure and assembly of β-amylase2 from Arabidopsis thaliana (2019)
Chandrasekharan N, Ravenburg C, Roy I, Monroe J, Berndsen C
RgGuinier 4.2 nm
Dmax 12.6 nm
VolumePorod 308 nm3

SASDGZ4Beta-amylase 2, chloroplastic (AtBAM2) Ndel1

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 215 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
Solution structure and assembly of β-amylase2 from Arabidopsis thaliana (2019)
Chandrasekharan N, Ravenburg C, Roy I, Monroe J, Berndsen C
RgGuinier 4.4 nm
Dmax 11.0 nm
VolumePorod 272 nm3

SASDUY9 – BAM2 in 100 mM KCl (0.25 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.9 nm
Dmax 16.4 nm
VolumePorod 226 nm3