Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ab initio only

SASDEN3 – Perivitellin PmPV2

P. maculata perivitellin 2 experimental SAS data

Sample:	P. maculata perivitellin 2 dimer, 188 kDa Pomacea maculata protein
Buffer:	20 mM Tris, pH: 7
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 Mar 26

Exaptation of two ancient immune proteins into a new dimeric pore-forming toxin in snails. J Struct Biol 211(2):107531 (2020)
Giglio ML, Ituarte S, Milesi V, Dreon MS, Brola TR, Caramelo J, Ip JCH, Maté S, Qiu JW, Otero LH, Heras H

R_g^Guinier	4.4	nm
D_max	14.3	nm
Volume^Porod	267	nm³

SASDDG3 – Solution Structure of Archaeal Biofilm Regulator 2 (AbfR2) in Complex with DNA

Sa0446 binding sequence 40bpTranscriptional regulator Lrs14-like protein experimental SAS data

Sample:	Sa0446 binding sequence 40bp monomer, 25 kDa DNA Transcriptional regulator Lrs14-like protein dimer, 33 kDa Sulfolobus acidocaldarius protein
Buffer:	300 mM NaCl, 20 mM HEPES, pH 7.5, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Nov 5

Solution Structure of Archaeal Biofilm Regulator 2 (AbfR2) in Complex with 40 bp DNA
Marian Vogt

R_g^Guinier	3.4	nm
D_max	12.8	nm
Volume^Porod	60	nm³

SASDE52 – Ribonuclease E from Escherichia coli

Endoribonuclease E experimental SAS data

Sample:	Endoribonuclease E tetramer, 247 kDa Escherichia coli protein
Buffer:	10 mM DTT, 10 mM MgCl2, 0.5 M NaCl, 20 mM Tris, pH: 8
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Feb 11

A structural and biochemical comparison of Ribonuclease E homologues from pathogenic bacteria highlights species-specific properties. Sci Rep 9(1):7952 (2019)
Mardle CE, Shakespeare TJ, Butt LE, Goddard LR, Gowers DM, Atkins HS, Vincent HA, Callaghan AJ

R_g^Guinier	5.0	nm
D_max	16.1	nm
Volume^Porod	468	nm³

SASDF96 – Olfactomedin-1 BMY isoform

Sample:	Noelin tetramer, 72 kDa Mus musculus protein
Buffer:	150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Feb 5

Design and structural characterisation of olfactomedin-1 variants as tools for functional studies. BMC Mol Cell Biol 20(1):50 (2019)
Pronker MF, van den Hoek H, Janssen BJC

R_g^Guinier	5.4	nm
D_max	16.3	nm
Volume^Porod	160	nm³

SASDFU4 – Conformation of R11-15 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data

Sample:	Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1

How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O

R_g^Guinier	6.2	nm
D_max	28.1	nm
Volume^Porod	144	nm³

SASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Sample:	Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1

R_g^Guinier	8.1	nm
D_max	29.6	nm
Volume^Porod	231	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

SASDFA6 – Proteolytic fragment of phage flagella binding tail protein YSD1_29 (amino acids 373-1296)

Flagella binding tail protein experimental SAS data

Sample:	Flagella binding tail protein monomer, 103 kDa Salmonella virus Chi protein
Buffer:	20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 4

The flagellotropic bacteriophage YSD1 targets Salmonella Typhi with a Chi-like protein tail fibre. Mol Microbiol (2019)
Dunstan RA, Pickard D, Dougan S, Goulding D, Cormie C, Hardy J, Li F, Grinter R, Harcourt K, Yu L, Song J, Schreiber F, Choudhary J, Clare S, Coulibaly F, Strugnell RA, Dougan G, Lithgow T

R_g^Guinier	5.6	nm
D_max	27.4	nm
Volume^Porod	155	nm³

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