Small Angle Scattering Biological Data Bank SASBDB

SASDEP5 – AMP-bound neanderthal adenylosuccinate lyase (ADSL)

Adenylosuccinate lyase experimental SAS data

Sample:	Adenylosuccinate lyase tetramer, 221 kDa Homo sapiens neanderthalensis protein
Buffer:	10 mM HEPES, 100 mM NaCl, 1 mM DTT, 1 mM AMP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Jul 24

Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase. Sci Rep 8(1):18008 (2018)
Van Laer B, Kapp U, Soler-Lopez M, Moczulska K, Pääbo S, Leonard G, Mueller-Dieckmann C

R_g^Guinier	3.7	nm
Volume^Porod	294	nm³

SASDEQ5 – AICAR-bound neanderthal adenylosuccinate lyase (ADSL)

Sample:	Adenylosuccinate lyase tetramer, 221 kDa Homo sapiens neanderthalensis protein
Buffer:	10 mM HEPES, 100 mM NaCl, 1 mM DTT, 1 mM 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Jul 24

Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase. Sci Rep 8(1):18008 (2018)
Van Laer B, Kapp U, Soler-Lopez M, Moczulska K, Pääbo S, Leonard G, Mueller-Dieckmann C

R_g^Guinier	3.7	nm
Volume^Porod	292	nm³

SASDER5 – AICAR/fumarate-bound neanderthal adenylosuccinate lyase (ADSL)

Sample:	Adenylosuccinate lyase tetramer, 221 kDa Homo sapiens neanderthalensis protein
Buffer:	10 mM HEPES, 100 mM NaCl, 1 mM DTT, 1 mM 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), 1mM Fumarate, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Jul 24

Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase. Sci Rep 8(1):18008 (2018)
Van Laer B, Kapp U, Soler-Lopez M, Moczulska K, Pääbo S, Leonard G, Mueller-Dieckmann C

R_g^Guinier	3.6	nm
Volume^Porod	252	nm³

SASDE96 – Aldehyde dehydrogenase 12 from Zea mays Extrapolated to Infinite Dilution

Aldehyde dehydrogenase 12 experimental SAS data

Sample:	Aldehyde dehydrogenase 12 tetramer, 242 kDa Zea mays protein
Buffer:	50 mM Tris-HCl, 50 mM NaCl, 0.5 mM TCEP, and 5% (v/v) glycerol, pH: 7.8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Dec 6

Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol (2018)
Korasick DA, Končitíková R, Kopečná M, Hájková E, Vigouroux A, Moréra S, Becker DF, Šebela M, Tanner JJ, Kopečný D

R_g^Guinier	4.1	nm
D_max	14.4	nm
Volume^Porod	351	nm³

SASDDM9 – lipoprotein lipase–GPIHBP1 complex

Lipoprotein lipaseGlycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 experimental SAS data

Sample:	Lipoprotein lipase dimer, 101 kDa Homo sapiens protein Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 dimer, 29 kDa Homo sapiens protein
Buffer:	10 mM BisTris, 150 mM NaCl, 4 mM CaCl2, 10% glycerol, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Dec 2

Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis. Proc Natl Acad Sci U S A (2018)
Birrane G, Beigneux AP, Dwyer B, Strack-Logue B, Kristensen KK, Francone OL, Fong LG, Mertens HDT, Pan CQ, Ploug M, Young SG, Meiyappan M

R_g^Guinier	5.5	nm
D_max	19.0	nm
Volume^Porod	319	nm³

SASDCR2 – Bromodomain-containing protein 4 (BRD4) tandem bromodomains

Bromodomain-containing protein 4 experimental SAS data

Sample:	Bromodomain-containing protein 4 monomer, 47 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Jan 13

Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains. Mol Cell (2018)
Lambert JP, Picaud S, Fujisawa T, Hou H, Savitsky P, Uusküla-Reimand L, Gupta GD, Abdouni H, Lin ZY, Tucholska M, Knight JDR, Gonzalez-Badillo B, St-Denis N, Newman JA, Stucki M, Pelletier L, Bandeira...

R_g^Guinier	6.3	nm
D_max	22.0	nm
Volume^Porod	251	nm³

SASDCS2 – Bromodomain-containing protein 3 (BRD3) tandem bromodomains

Bromodomain-containing protein 3 experimental SAS data

Sample:	Bromodomain-containing protein 3 monomer, 44 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Jan 13

R_g^Guinier	6.2	nm
D_max	21.5	nm
Volume^Porod	210	nm³

SASDCT2 – Bromodomain-containing protein 2 (BRD2) tandem bromodomains

Bromodomain-containing protein 2 experimental SAS data

Sample:	Bromodomain-containing protein 2 monomer, 43 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Jan 13

R_g^Guinier	5.7	nm
D_max	21.0	nm
Volume^Porod	220	nm³

SASDCU2 – Bromodomain testis-specific protein (BRDT) tandem bromodomains

Bromodomain testis-specific protein experimental SAS data

Sample:	Bromodomain testis-specific protein monomer, 43 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Jan 13

R_g^Guinier	5.1	nm
D_max	20.0	nm
Volume^Porod	200	nm³

SASDEZ6 – Gamma-crystallin S disulfide-linked dimer

Gamma-crystallin S experimental SAS data

Sample:	Gamma-crystallin S dimer, 42 kDa Homo sapiens protein
Buffer:	20 mM sodium phosphate, pH: 7
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23

The structure and stability of the disulfide-linked γS-crystallin dimer provide insight into oxidation products associated with lens cataract formation. J Mol Biol (2018)
Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA

R_g^Guinier	2.4	nm
D_max	7.5	nm
Volume^Porod	45	nm³

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