Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDGR4 – Human alpha-aminoadipic semialdehyde dehydrogenase (ALDH)7A1 E399D at 5.7 mg/mL

Alpha-aminoadipic semialdehyde dehydrogenase E399D experimental SAS data

Sample:	Alpha-aminoadipic semialdehyde dehydrogenase E399D, 56 kDa Homo sapiens protein
Buffer:	50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1

Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy. J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ

R_g^Guinier	3.9	nm
D_max	10.6	nm
Volume^Porod	272	nm³

SASDGS4 – Human alpha-aminoadipic semialdehyde dehydrogenase (ALDH)7A1 E399G at 1.6 mg/mL

Alpha-aminoadipic semialdehyde dehydrogenase E399G experimental SAS data

Sample:	Alpha-aminoadipic semialdehyde dehydrogenase E399G, 55 kDa Homo sapiens protein
Buffer:	50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1

R_g^Guinier	3.8	nm
D_max	11.3	nm
Volume^Porod	290	nm³

SASDGT4 – Human alpha-aminoadipic semialdehyde dehydrogenase (ALDH)7A1 E399G at 3.2 mg/mL

Sample:	Alpha-aminoadipic semialdehyde dehydrogenase E399G, 55 kDa Homo sapiens protein
Buffer:	50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1

R_g^Guinier	3.7	nm
D_max	10.6	nm
Volume^Porod	250	nm³

SASDGU4 – Human alpha-aminoadipic semialdehyde dehydrogenase (ALDH)7A1 E399G at 6.5 mg/mL

Sample:	Alpha-aminoadipic semialdehyde dehydrogenase E399G, 55 kDa Homo sapiens protein
Buffer:	50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1

R_g^Guinier	3.8	nm
D_max	10.0	nm
Volume^Porod	270	nm³

SASDGX4 – Aryl-hydrocarbon-interacting protein-like 1

Aryl-hydrocarbon-interacting protein-like 1(1-316) experimental SAS data

Aryl-hydrocarbon-interacting protein-like 1(1-316) Kratky plot

Sample:	Aryl-hydrocarbon-interacting protein-like 1(1-316) monomer, 37 kDa Homo sapiens protein
Buffer:	50 mM Tris, 100 mM NaCl, 2.5 % glycerol and 6 mM DTT, pH: 7.5
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jul 17

Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor-interacting protein-like 1 with the regulatory Pγ subunit of phosphodiesterase 6. J Biol Chem 294(43):15795-15807 (2019)
Yadav RP, Boyd K, Yu L, Artemyev NO

R_g^Guinier	2.6	nm
D_max	9.1	nm
Volume^Porod	60	nm³

SASDFL4 – C-type lectins CTL4/CTLMA2, 3.1 mg/ml

AGAP005335-PAAGAP005334-PA experimental SAS data

Sample:	AGAP005335-PA monomer, 18 kDa Anopheles gambiae protein AGAP005334-PA monomer, 18 kDa Anopheles gambiae protein
Buffer:	500 mM NaCl, 20 mM CHES, 0.5 mM CaCl2, 1% glycerol, pH: 9
Experiment:	SAXS data collected at Rigaku BioSAXS-2000, Thomas Jefferson University on 2018 Aug 30

Solution structure, glycan specificity and of phenol oxidase inhibitory activity of Anopheles C-type lectins CTL4 and CTLMA2. Sci Rep 9(1):15191 (2019)
Bishnoi R, Sousa GL, Contet A, Day CJ, Hou CD, Profitt LA, Singla D, Jennings MP, Valentine AM, Povelones M, Baxter RHG

R_g^Guinier	2.5	nm
D_max	8.0	nm
Volume^Porod	58	nm³

SASDGV6 – Cysteine synthase A

Cysteine synthase A experimental SAS data

Sample:	Cysteine synthase A dimer, 71 kDa Escherichia coli protein
Buffer:	20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment:	SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1

Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. Int J Mol Sci 20(20) (2019)
Rosa B, Marchetti M, Paredi G, Amenitsch H, Franko N, Benoni R, Giabbai B, De Marino MG, Mozzarelli A, Ronda L, Storici P, Campanini B, Bettati S

R_g^Guinier	2.6	nm
D_max	8.5	nm
Volume^Porod	108	nm³

SASDGW6 – Serine acetyltransferase

Serine acetyltransferase experimental SAS data

Sample:	Serine acetyltransferase hexamer, 177 kDa Escherichia coli protein
Buffer:	20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment:	SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1

R_g^Guinier	3.9	nm
D_max	13.0	nm
Volume^Porod	280	nm³

SASDGX6 – Cysteine synthase/Serine acetyltransferase complex

Cysteine synthase A (4-mer)Serine acetyltransferase (6-mer) experimental SAS data

Sample:	Cysteine synthase A (4-mer) tetramer, 143 kDa Escherichia coli protein Serine acetyltransferase (6-mer) hexamer, 177 kDa Escherichia coli protein
Buffer:	20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment:	SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1

R_g^Guinier	6.1	nm
D_max	22.0	nm
Volume^Porod	457	nm³

SASDFT9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S2 (-ss) ECR

Adhesion G-protein coupled receptor G6 S2 experimental SAS data

Adhesion G-protein coupled receptor G6 S2 Kratky plot

Sample:	Adhesion G-protein coupled receptor G6 S2 monomer, 86 kDa Danio rerio protein
Buffer:	150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28

Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D

R_g^Guinier	4.0	nm
D_max	14.1	nm
Volume^Porod	169	nm³

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