Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: No model

SASDGB3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 4.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data

80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K Kratky plot

Sample:	80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA 80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA DNA-binding protein HU-alpha, E34K dimer, 19 kDa Escherichia coli protein
Buffer:	10 mM sodium acetate, 50 mM NaCl, pH: 4.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2

Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDGC3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 5.5)

Sample:	80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA 80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA DNA-binding protein HU-alpha, E34K dimer, 19 kDa Escherichia coli protein
Buffer:	10 mM Bis-Tris, 50 mM NaCl, pH: 5.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2

SASDGD3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 6.5)

Sample:	80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA 80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA DNA-binding protein HU-alpha, E34K, 100 kDa Escherichia coli protein
Buffer:	10mM Bis-Tris, 50 mM NaCl, pH: 6.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2

R_g^Guinier	7.3	nm
D_max	28.0	nm
Volume^Porod	330	nm³

SASDGE3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 7.5)

Sample:	80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA 80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA DNA-binding protein HU-alpha, E34K, 100 kDa Escherichia coli protein
Buffer:	10 mM Bis-Tris, 50 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2

R_g^Guinier	7.1	nm
D_max	27.5	nm
Volume^Porod	309	nm³

SASDG85 – Wild-type full-length Liver Receptor Homolog-1/Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha peptide complex bound to the CYP7A1 promoter oligonucleotide duplex.

Liver Receptor Homolog-1Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 AlphaCYP7A1 Promoter ForwardCYP7A1 Promoter Reverse experimental SAS data

Sample:	Liver Receptor Homolog-1 monomer, 64 kDa Homo sapiens protein Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha monomer, 2 kDa Homo sapiens protein CYP7A1 Promoter Forward monomer, 4 kDa Homo sapiens DNA CYP7A1 Promoter Reverse monomer, 4 kDa Homo sapiens DNA
Buffer:	20 mM TRIS, 150 mM NaCl, 2% v/v glycerol, 0.5 mM CHAPS, 5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 26

Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function. Structure (2020)
Seacrist CD, Kuenze G, Hoffmann RM, Moeller BE, Burke JE, Meiler J, Blind RD

R_g^Guinier	3.8	nm
D_max	13.0	nm
Volume^Porod	76	nm³

SASDEX4 – Herpes simplex virus 1 tegument protein UL11

Cytoplasmic envelopment protein 3 experimental SAS data

Cytoplasmic envelopment protein 3 Kratky plot

Sample:	Cytoplasmic envelopment protein 3 monomer, 12 kDa Human alphaherpesvirus 1 protein
Buffer:	50 mM HEPES, 100 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine (TCEP),, pH: 7.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 4

Conserved Outer Tegument Component UL11 from Herpes Simplex Virus 1 Is an Intrinsically Disordered, RNA-Binding Protein. mBio 11(3) (2020)
Metrick CM, Koenigsberg AL, Heldwein EE

R_g^Guinier	2.4	nm
D_max	12.0	nm
Volume^Porod	30	nm³

SASDJ73 – Ubiquitin-like UHRF1 with PHD and RING finger domains (TTD-L2 (123-301))

E3 ubiquitin-protein ligase UHRF1 experimental SAS data

E3 ubiquitin-protein ligase UHRF1 Kratky plot

Sample:	E3 ubiquitin-protein ligase UHRF1 monomer, 21 kDa Homo sapiens protein
Buffer:	SAXS Buffer, pH: 7.5
Experiment:	SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 Nov 26

Serine 298 Phosphorylation in Linker 2 of UHRF1 Regulates Ligand-Binding Property of its Tandem Tudor Domain Journal of Molecular Biology (2020)
Kori S, Jimenji T, Ekimoto T, Sato M, Kusano F, Oda T, Unoki M, Ikeguchi M, Arita K

R_g^Guinier	2.0	nm
D_max	6.6	nm
Volume^Porod	26	nm³

SASDJ83 – Phosphorylated ubiquitin-like UHRF1 with PHD and RING finger domains (phTTD-L2 (123-301)

Sample:	E3 ubiquitin-protein ligase UHRF1 monomer, 21 kDa Homo sapiens protein
Buffer:	SAXS buffer, pH: 7.5
Experiment:	SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 Nov 26

R_g^Guinier	2.1	nm
D_max	7.0	nm
Volume^Porod	29	nm³

SASDHT4 – Phosphoprotein from Nipah virus

Sample:	Phosphoprotein tetramer, 317 kDa Nipah henipavirus protein
Buffer:	20 mM Tris-HCL, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at ID14-3, ESRF on 2011 Nov 3

Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1. Biophys J (2020)
Jensen MR, Yabukarski F, Communie G, Condamine E, Mas C, Volchkova V, Tarbouriech N, Bourhis JM, Volchkov V, Blackledge M, Jamin M

R_g^Guinier	10.9	nm
D_max	39.3	nm

SASDHK8 – Ile-Leu-Gln-Ile-Asn-Ser (ILQINS) hexapeptide self-assembly (2019-dataset)

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data

Ile-Leu-Gln-Ile-Asn-Ser peptide Kratky plot

Sample:	Ile-Leu-Gln-Ile-Asn-Ser peptide, 1 kDa synthetic construct protein
Buffer:	pure (MQ, 18 MΩ) Water, pH: 7
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 1

Amyloid Evolution: Antiparallel Replaced by Parallel. Biophys J (2020)
Zanjani AAH, Reynolds NP, Zhang A, Schilling T, Mezzenga R, Berryman JT

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