SASBDB entries for UniProt ID:

SASDGW5 – Suppressor of Fused from Drosophila

UniProt ID: Q9VG38 (1-468) Suppressor of fused homolog
Suppressor of fused homolog experimental SAS data
CUSTOM IN-HOUSE model
Sample: Suppressor of fused homolog monomer, 53 kDa Drosophila melanogaster protein
Buffer: 50 mM bis-TRIS pH 5.5, 200 mM NaCl, 10% glycerol, pH: 5.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 May 7
Suppressor of Fused
Valerie Biou
RgGuinier 2.7 nm
Dmax 8.8 nm
VolumePorod 12 nm3

SASDGZ5 – Suppressor of Fused from Human D30

UniProt ID: Q9UMX1 (None-None) Suppressor of fused homolog
Suppressor of fused homolog experimental SAS data
CUSTOM IN-HOUSE model
Sample: Suppressor of fused homolog monomer, 51 kDa Homo sapiens protein
Buffer: 50 mM bis-TRIS pH 5.5, 200 mM NaCl, 10% glycerol, pH: 5.5
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Jun 30
Suppressor of Fused
Valerie Biou
RgGuinier 3.2 nm
Dmax 14.0 nm

SASDG26 – Wild type 4-hydroxy-tetrahydrodipicolinate synthase

UniProt ID: Q9PPB4 (1-298) 4-hydroxy-tetrahydrodipicolinate synthase
4-hydroxy-tetrahydrodipicolinate synthase experimental SAS data
DAMFILT model
Sample: 4-hydroxy-tetrahydrodipicolinate synthase tetramer, 131 kDa Campylobacter jejuni protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Aug 2
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J Struct Biol :107409 (2019)
Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ
RgGuinier 3.4 nm
Dmax 9.0 nm
VolumePorod 188 nm3

SASDG36 – 4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant)

UniProt ID: Q9PPB4 (1-298) 4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant)
4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant) experimental SAS data
DAMFILT model
Sample: 4-hydroxy-tetrahydrodipicolinate synthase (N84D mutant) dimer, 65 kDa Campylobacter jejuni protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Aug 2
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J Struct Biol :107409 (2019)
Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ
RgGuinier 3.1 nm
Dmax 9.5 nm
VolumePorod 108 nm3

SASDG46 – 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)

UniProt ID: Q9PPB4 (1-298) 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)
4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant) experimental SAS data
DAMFILT model
Sample: 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant), 33 kDa Campylobacter jejuni protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Aug 2
Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J Struct Biol :107409 (2019)
Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ
RgGuinier 3.3 nm
Dmax 8.9 nm
VolumePorod 163 nm3

SASDGB6 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8A) miniGi complex

UniProt ID: Q5E9J8 (1-492) Resistance to inhibitors of cholinesterase 8 homolog A

UniProt ID: None (None-None) miniGi
Resistance to inhibitors of cholinesterase 8 homolog AminiGi experimental SAS data
OTHER model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Bos taurus protein
MiniGi monomer, 25 kDa synthetic construct 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
Large-scale conformational rearrangement of the α5-helix of Gα subunits in complex with the guanine nucleotide exchange factor Ric8A. J Biol Chem (2019)
Srivastava D, Artemyev NO
RgGuinier 3.2 nm
Dmax 10.7 nm

SASDGC6 – Glucuronoyl esterase, deglycolsylated full length

UniProt ID: A0A0A7EQR3 (18-474) 4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase)
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) experimental SAS data
DAMMIN model
Sample: 4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) monomer, 51 kDa Cerrena unicolor protein
Buffer: 20 mM sodium acetate, pH: 5
Experiment: SAXS data collected at Xenocs BioXolver L with GeniX3D, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Oct 10
The structural basis of fungal glucuronoyl esterase activity on natural substrates. Nat Commun 11(1):1026 (2020)
Ernst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Agger JW, Larsen S
RgGuinier 3.2 nm
Dmax 11.0 nm
VolumePorod 71 nm3

SASDGD6 – Glucuronoyl esterase S286A, deglycolsylated truncated (amino acids 95-474)

UniProt ID: A0A0A7EQR3 (95-474) 4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase, truncated)
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase, truncated) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase, truncated) monomer, 43 kDa Cerrena unicolor protein
Buffer: 20 mM sodium acetate, pH: 5
Experiment: SAXS data collected at Xenocs BioXolver L with GeniX3D, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Oct 10
The structural basis of fungal glucuronoyl esterase activity on natural substrates. Nat Commun 11(1):1026 (2020)
Ernst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Agger JW, Larsen S
RgGuinier 2.0 nm
Dmax 6.1 nm
VolumePorod 50 nm3

SASDGV6 – Cysteine synthase A

UniProt ID: P0ABK5 (1-323) Cysteine synthase A
Cysteine synthase A experimental SAS data
DAMMIN model
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
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 108 nm3

SASDGW6 – Serine acetyltransferase

UniProt ID: P0A9D4 (2-273) Serine acetyltransferase
Serine acetyltransferase experimental SAS data
DAMMIF model
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
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
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 280 nm3