Small Angle Scattering Biological Data Bank SASBDB

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12 hits found for Beta-amylase

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

R_g^Guinier	4.9	nm
D_max	15.0	nm
Volume^Porod	234	nm³

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

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

R_g^Guinier	4.7	nm
D_max	15.1	nm
Volume^Porod	218	nm³

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

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

R_g^Guinier	4.7	nm
D_max	15.0	nm
Volume^Porod	220	nm³

SASDA62 – bAmylase in PBS

Sample:	Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer:	PBS, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 20

Standard proteins
Darja Ruskule

R_g^Guinier	4.2	nm
D_max	12.7	nm
Volume^Porod	214	nm³

SASDGY4 – Beta-amylase 2, chloroplastic (AtBAM2)

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

R_g^Guinier	4.2	nm
D_max	12.6	nm
Volume^Porod	308	nm³

SASDGZ4 – Beta-amylase 2, chloroplastic (AtBAM2) Ndel1

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

R_g^Guinier	4.4	nm
D_max	11.0	nm
Volume^Porod	272	nm³

SASDMX5 – ...beta-amylase (ZmBAM7) short

Sample:	Beta-amylase tetramer, 231 kDa Zea mays protein
Buffer:	50 mM HEPES, 25 mM NaCl, and 0.2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7

The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C

R_g^Guinier	5.3	nm
D_max	16.3	nm
Volume^Porod	615	nm³

SASDMY5 – ...beta-amylase (ZmBAM7) short

Sample:	Beta-amylase tetramer, 231 kDa Zea mays protein
Buffer:	50 mM HEPES, 25 mM NaCl, and 0.2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7

R_g^Guinier	5.1	nm
D_max	13.9	nm
Volume^Porod	467	nm³

SASDMZ5 – ...beta-amylase 1

Beta-amylase 1, chloroplastic experimental SAS data

Sample:	Beta-amylase 1, chloroplastic monomer, 65 kDa Arabidopsis thaliana protein
Buffer:	50 mM MES, 100 mM NaCl, 1 mM DTT, pH: 6.7
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 22

R_g^Guinier	2.6	nm
D_max	9.8	nm
Volume^Porod	88	nm³

SASDM26 – ...beta-amylase 5

Sample:	Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer:	20 mM HEPES, 150 mM NaCl, and 0.2 mM TCEP, pH: 7.3
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7

R_g^Guinier	4.4	nm
D_max	14.1	nm
Volume^Porod	296	nm³

SASDCE8 – Beta amylase from sweet potato (WAXS)

Sample:	Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer:	tbs, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2015 Jul 15

WAXS benchmark on standard proteins
Maxim Petoukhov

R_g^Guinier

4.0

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

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

R_g^Guinier	4.9	nm
D_max	16.4	nm
Volume^Porod	226	nm³