Small Angle Scattering Biological Data Bank SASBDB

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SASDK47 – SANS data for the sensory rhodopsin II / transducer complex in detergent at 1.4 M NaCl

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data

Sample:	Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer:	1400 mM NaCl, 49.4 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment:	SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Feb 10

Molecular model of a sensor of two-component signaling system Scientific Reports 11(1) (2021)
Ryzhykau Y, Orekhov P, Rulev M, Vlasov A, Melnikov I, Volkov D, Nikolaev M, Zabelskii D, Murugova T, Chupin V, Rogachev A, Gruzinov A, Svergun D, Brennich M, Gushchin I, Soler-Lopez M, Bothe A, Büldt G, Leonard G, Engelhard M, Kuklin A, Gordeliy V

R_g^Guinier	9.9	nm
D_max	36.5	nm

SASDK57 – SANS data for the sensory rhodopsin II / transducer complex in detergent at 2.8 M NaCl

Sample:	Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer:	2800 mM NaCl, 76.6 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment:	SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Feb 10

R_g^Guinier	9.3	nm
D_max	37.5	nm

SASDK67 – SANS data for the sensory rhodopsin II / transducer complex in detergent at 4.0 M NaCl

Sample:	Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer:	4000 mM NaCl, 100 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment:	SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Jan 25

R_g^Guinier	8.9	nm
D_max	39.0	nm

SASDK24 – Signal recognition particle SRP9/14 heterodimer from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14 experimental SAS data

Sample:	Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein
Buffer:	20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2018 Feb 22

Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I

R_g^Guinier	2.1	nm
D_max	7.2	nm
Volume^Porod	47	nm³

SASDK34 – Full length SRP Alu RNA from Plasmodium falciparum

Full-length SRP Alu RNA experimental SAS data

Sample:	Full-length SRP Alu RNA monomer, 38 kDa Plasmodium falciparum RNA
Buffer:	20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2018 Jun 22

R_g^Guinier	3.3	nm
D_max	11.8	nm
Volume^Porod	63	nm³

SASDK44 – The 5' domain of SRP Alu RNA from Plasmodium falciparum

SRP Alu RNA 5' domain experimental SAS data

Sample:	SRP Alu RNA 5' domain monomer, 24 kDa Plasmodium falciparum RNA
Buffer:	20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2018 Jun 22

R_g^Guinier	3.3	nm
D_max	11.5	nm
Volume^Porod	38	nm³

SASDK54 – Signal recognition particle SRP9/14 heterodimer in complex with full length SRP Alu RNA from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14Full-length SRP Alu RNA experimental SAS data

Sample:	Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein Full-length SRP Alu RNA monomer, 38 kDa Plasmodium falciparum RNA
Buffer:	20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2018 Jun 22

R_g^Guinier	3.5	nm
D_max	12.0	nm
Volume^Porod	120	nm³

SASDK64 – Signal recognition particle SRP9/14 heterodimer in complex with the 5' domain of SRP Alu RNA from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14SRP Alu RNA 5' domain experimental SAS data

Sample:	Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein SRP Alu RNA 5' domain monomer, 24 kDa Plasmodium falciparum RNA
Buffer:	20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2018 Jun 22

R_g^Guinier	3.2	nm
D_max	11.9	nm
Volume^Porod	77	nm³

SASDJU7 – HIV-1 Primer Binding Site (PBS)-Segment RNA

Primer Binding Site-Segment experimental SAS data

Sample:	Primer Binding Site-Segment monomer, 33 kDa HIV-1: pNL4-3 RNA
Buffer:	10 mM Tris, 140 mM KCl, 10 mM NaCl, 1 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Jul 29

The three-way junction structure of the HIV-1 PBS-segment binds host enzyme important for viral infectivity. Nucleic Acids Res (2021)
Song Z, Gremminger T, Singh G, Cheng Y, Li J, Qiu L, Ji J, Lange MJ, Zuo X, Chen SJ, Zou X, Boris-Lawrie K, Heng X

R_g^Guinier	3.4	nm
D_max	12.8	nm
Volume^Porod	87	nm³

SASDLJ3 – SH3 and multiple ankyrin repeat domains protein 3 (wild type)

SH3 and multiple ankyrin repeat domains protein 3 experimental SAS data

Sample:	SH3 and multiple ankyrin repeat domains protein 3 monomer, 88 kDa Rattus norvegicus protein
Buffer:	100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3

Autism associated SHANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses. Elife 10 (2021)
Bucher M, Niebling S, Han Y, Molodenskiy D, Nia FH, Kreienkamp HJ, Svergun D, Kim E, Kostyukova AS, Kreutz MR, Mikhaylova M

R_g^Guinier	4.1	nm
D_max	14.0	nm
Volume^Porod	170	nm³

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