Small Angle Scattering Biological Data Bank SASBDB

Browse by ORGANISM: Homo sapiens (Human)

SASDNB3 – Homodimerisation of the CP110 C-terminus coiled-coil domain

Centriolar coiled-coil protein of 110 kDa experimental SAS data

Sample:	Centriolar coiled-coil protein of 110 kDa dimer, 20 kDa Homo sapiens protein
Buffer:	50 mM HEPES, pH 7.5, 100 mM NaCl, 1 mM DTT, 1 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Feb 23

Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends. J Cell Biol 224(3) (2025)
Iyer SS, Chen F, Ogunmolu FE, Moradi S, Volkov VA, van Grinsven EJ, van Hoorn C, Wu J, Andrea N, Hua S, Jiang K, Vakonakis I, Potočnjak M, Herzog F, Gigant B, Gudimchuk N, Stecker KE, Dogterom M, Steinmetz MO, Akhmanova A

R_g^Guinier	3.5	nm
D_max	12.5	nm
Volume^Porod	33	nm³

SASDMS6 – Non-POU domain-containing octamer-binding protein (NONO homodimer)

Non-POU domain-containing octamer-binding protein experimental SAS data

Sample:	Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris-Cl (pH 7.5), 250 mM KCl, 50 mM L-proline, 0.5 mM EDTA, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28

Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1. Nucleic Acids Res (2021)
Knott GJ, Chong YS, Passon DM, Liang XH, Deplazes E, Conte MR, Marshall AC, Lee M, Fox AH, Bond CS

R_g^Guinier	2.8	nm
D_max	9.5	nm
Volume^Porod	96	nm³

SASDMT6 – Non-POU domain-containing octamer-binding protein (NONO homodimer) bound to an antisense oligonucleotide

Non-POU domain-containing octamer-binding protein5-10-5 gapmer phosphorothioate antisense oligonucleotide tetramer experimental SAS data

Sample:	Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein 5-10-5 gapmer phosphorothioate antisense oligonucleotide tetramer tetramer, 28 kDa
Buffer:	20 mM Tris-Cl (pH 7.5), 250 mM KCl, 50 mM L-proline, 0.5 mM EDTA, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28

R_g^Guinier	3.9	nm
D_max	18.4	nm
Volume^Porod	153	nm³

SASDMM7 – Apo-serotransferrin at pH 5.5

Sample:	Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer:	15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl, (APO Buffer), pH: 5.5
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 7

X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin International Journal of Molecular Sciences 22(24):13392 (2021)
Campos-Escamilla C, Siliqi D, Gonzalez-Ramirez L, Lopez-Sanchez C, Gavira J, Moreno A

R_g^Guinier	3.1	nm
D_max	9.8	nm
Volume^Porod	106	nm³

SASDMN7 – Apo-serotransferrin at pH 7.0

Sample:	Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer:	15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (APO Buffer), pH: 7
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 7

R_g^Guinier	3.1	nm
D_max	9.6	nm
Volume^Porod	106	nm³

SASDMP7 – Apo-serotransferrin at pH 8.0

Sample:	Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer:	15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (Buffer APO-Tf-1), pH: 8
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 7

R_g^Guinier	3.1	nm
D_max	9.4	nm
Volume^Porod	106	nm³

SASDMQ7 – HOLO-serotransferrin at pH 5.5 in the presence of iron

Sample:	Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer:	15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl, (APO Buffer), pH: 5.5
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 7

R_g^Guinier	3.3	nm
D_max	14.6	nm
Volume^Porod	107	nm³

SASDMR7 – HOLO-serotransferrin at pH 7.0 in the presence of iron

Sample:	Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer:	15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (APO Buffer), pH: 7
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 7

R_g^Guinier	3.2	nm
D_max	13.5	nm
Volume^Porod	103	nm³

SASDMS7 – HOLO-serotransferrin at pH 8.0 in the presence of iron

Sample:	Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer:	15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (Buffer APO-Tf-1), pH: 8
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 7

R_g^Guinier	3.2	nm
D_max	13.1	nm
Volume^Porod	106	nm³

SASDKV7 – CCP2-SP domains of the complement C1r subcomponent

Complement C1r subcomponent experimental SAS data

Sample:	Complement C1r subcomponent monomer, 38 kDa Homo sapiens protein
Buffer:	10 mM HEPES, 140 mM NaCl, pH: 7.3
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 24

A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes. J Immunol 207(11):2856-2867 (2021)
Garrigues RJ, Powell-Pierce AD, Hammel M, Skare JT, Garcia BL

R_g^Guinier	2.4	nm
D_max	7.9	nm
Volume^Porod	63	nm³

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