Small Angle Scattering Biological Data Bank SASBDB

Browse by ORGANISM: Homo sapiens (Human)

SASDHF8 – Histatin 5 (Histatin 3; His3-(20-43)-peptide) at 4.89 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K

Histatin-3, His3-(20-43)-peptide experimental SAS data

Histatin 5 (Histatin 3; His3-(20-43)-peptide) at 4.89 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K Rg histogram

Sample:	Histatin-3, His3-(20-43)-peptide monomer, 3 kDa Homo sapiens protein
Buffer:	20 mM Tris, 150 mM NaCl,, pH: 7
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2020 Mar 13

Comment on the Optimal Parameters to Derive Intrinsically Disordered Protein Conformational Ensembles from Small-Angle X-ray Scattering Data Using the Ensemble Optimization Method Journal of Chemical Theory and Computation (2021)
Sagar A, Jeffries C, Petoukhov M, Svergun D, Bernadó P

R_g^Guinier	1.4	nm
D_max	6.0	nm
Volume^Porod	3	nm³

SASDHG8 – Histatin 5 (Histatin 3; His3-(20-43)-peptide) at 2.51 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K

Histatin-3, His3-(20-43)-peptide Kratky plot

Sample:	Histatin-3, His3-(20-43)-peptide monomer, 3 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl, pH: 7
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2020 Mar 13

R_g^Guinier	1.5	nm
D_max	6.4	nm
Volume^Porod	3	nm³

SASDHH8 – Histatin 5 (Histatin 3; His3-(20-43)-peptide) at 1.26 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K

Sample:	Histatin-3, His3-(20-43)-peptide monomer, 3 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl, pH: 7
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2020 Mar 13

R_g^Guinier	1.5	nm
D_max	6.0	nm
Volume^Porod	3	nm³

SASDKL4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 10 mg/ml)

Serine protease HTRA2, mitochondrial experimental SAS data

Sample:	Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer:	20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1

Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR Proceedings of the National Academy of Sciences 118(11):e2025022118 (2021)
Toyama Y, Harkness R, Lee T, Maynes J, Kay L

R_g^Guinier	4.2	nm
D_max	16.0	nm
Volume^Porod	250	nm³

SASDKM4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 5 mg/ml)

Sample:	Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer:	20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1

R_g^Guinier	3.8	nm
D_max	15.0	nm
Volume^Porod	213	nm³

SASDKN4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 2 mg/ml)

Sample:	Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer:	20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1

R_g^Guinier	3.6	nm
D_max	12.8	nm
Volume^Porod	203	nm³

SASDKP4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 1 mg/ml)

Sample:	Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer:	20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1

R_g^Guinier	3.4	nm
D_max	12.0	nm
Volume^Porod	168	nm³

SASDJ64 – Calcium bound Calmodulin

Sample:	Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 4 mM CaCl₂, pH: 7.4
Experiment:	SAXS data collected at SWING, SOLEIL on 2016 Sep 24

A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells Advanced Science :2003630 (2021)
Voegele A, Sadi M, O'Brien D, Gehan P, Raoux‐Barbot D, Davi M, Hoos S, Brûlé S, Raynal B, Weber P, Mechaly A, Haouz A, Rodriguez N, Vachette P, Durand D, Brier S, Ladant D, Chenal A

R_g^Guinier	2.2	nm
D_max	7.3	nm
Volume^Porod	27	nm³

SASDJ74 – P454 peptide from B.pertussis CyaA toxin complexed with calmodulin

Calmodulin-1Bifunctional hemolysin/adenylate cyclase experimental SAS data

Sample:	Calmodulin-1 monomer, 17 kDa Homo sapiens protein Bifunctional hemolysin/adenylate cyclase monomer, 3 kDa Bordetella pertussis protein
Buffer:	20 mM HEPES, 150 mM NaCl, 4 mM CaCl₂, pH: 7.4
Experiment:	SAXS data collected at SWING, SOLEIL on 2016 Sep 24

R_g^Guinier	2.0	nm
D_max	7.0	nm
Volume^Porod	28	nm³

SASDKB8 – Immunoglobulin G1 (IgG1) Glycosylated

Immunoglobulin G subclass 1 experimental SAS data

Sample:	Immunoglobulin G subclass 1, 148 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Oct 20

Solution structure of deglycosylated human IgG1 shows the role of CH2 glycans in its conformation Biophysical Journal (2021)
Spiteri V, Doutch J, Rambo R, Gor J, Dalby P, Perkins S

R_g^Guinier	5.1	nm
D_max	17.5	nm
Volume^Porod	269	nm³

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