Small Angle Scattering Biological Data Bank SASBDB

SASDF56 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 150 mM NaCl

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

80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha 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 , 10 kDa Escherichia coli protein
Buffer:	10 mM sodium acetate, 150 mM NaCl, pH: 4.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1

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

SASDF66 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 300 mM NaCl

Sample:	80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA 80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer:	10 mM sodium acetate, 300 mM NaCl, pH: 4.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1

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

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

SASDFW7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆328-352 (MCoA∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) experimental SAS data

Sample:	Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer:	50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2017 Jul 13

The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L

R_g^Guinier	2.3	nm
D_max	6.9	nm
Volume^Porod	77	nm³

SASDFX7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆337-346 (MCoA∆337-346)

Aquifex aeolicus McoA metaloxidase ∆337-346 experimental SAS data

Sample:	Aquifex aeolicus McoA metaloxidase ∆337-346 monomer, 54 kDa Aquifex aeolicus protein
Buffer:	50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Dec 4

R_g^Guinier	2.3	nm
D_max	7.0	nm
Volume^Porod	78	nm³

SASDFY7 – Aquifex aeolicus McoA metaloxidase

Aquifex aeolicus McoA metaloxidase experimental SAS data

Sample:	Aquifex aeolicus McoA metaloxidase monomer, 55 kDa Aquifex aeolicus protein
Buffer:	50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Apr 15

R_g^Guinier	2.3	nm
D_max	7.5	nm
Volume^Porod	79	nm³

SASDH92 – Plasmodium falciparum lipocalin (PF3D7_0925900): Dimer-tetramer equilibrium through a concentration series (combined batch and SEC-SAXS measurements)

Plasmodium falciparum Lipocalin experimental SAS data

Sample:	Plasmodium falciparum Lipocalin tetramer, 89 kDa Plasmodium falciparum protein
Buffer:	20 mM Tris pH7.5, 150 mM NaCl, 5% v/v glycerol, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 Apr 8

Structure-Based Identification and Functional Characterization of a Lipocalin in the Malaria Parasite Plasmodium falciparum Cell Reports 31(12):107817 (2020)
Burda P, Crosskey T, Lauk K, Zurborg A, Söhnchen C, Liffner B, Wilcke L, Pietsch E, Strauss J, Jeffries C, Svergun D, Wilson D, Wilmanns M, Gilberger T

R_g^Guinier	3.2	nm
D_max	10.3	nm
Volume^Porod	126	nm³

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