Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ab initio only

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

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	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

SASDJS5 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-monomer

Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data

Sample:	Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial monomer, 70 kDa Saccharomyces cerevisiae protein
Buffer:	40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 May 1

Expression and analysis of the SAM-dependent RNA methyltransferase Rsm22 from Saccharomyces cerevisiae Acta Crystallographica Section D Structural Biology 77(6) (2021)
Alam J, Rahman F, Sah-Teli S, Venkatesan R, Koski M, Autio K, Hiltunen J, Kastaniotis A

R_g^Guinier	3.8	nm
D_max	13.9	nm
Volume^Porod	160	nm³

SASDJT5 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-dimer

dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data

Sample:	Dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial dimer, 141 kDa Saccharomyces cerevisiae protein
Buffer:	40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 May 1

R_g^Guinier	5.0	nm
D_max	18.2	nm
Volume^Porod	516	nm³

SASDEC6 – Adenylation Domain of DNA ligase A with NAD+

Sample:	DNA ligase A monomer, 38 kDa Mycobacterium tuberculosis protein
Buffer:	50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2018 Oct 6

Salt bridges at the subdomain interfaces of the adenylation domain and active-site residues of Mycobacterium tuberculosis NAD ⁺ -dependent DNA ligase A (MtbLigA) are important for the initial steps of nick-sealing activity Acta Crystallographica Section D Structural Biology 77(6) (2021)
Afsar M, Shukla A, Kumar N, Ramachandran R

R_g^Guinier	2.4	nm
D_max	6.2	nm
Volume^Porod	94	nm³

SASDG65 – Adenylation domain of DNA ligase A (LigA)

Sample:	DNA ligase A monomer, 37 kDa Mycobacterium tuberculosis protein
Buffer:	50 mM Tris-HCl 200 mM NaCl 2mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 May 21

R_g^Guinier	2.7	nm
D_max	8.9	nm
Volume^Porod	68	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

SASDKN8 – Rationally optimised WA20 (ROWA) tetramer

Rationally optimised WA20 mutant N22A/H86K (ROWA) tetramer experimental SAS data

Sample:	Rationally optimised WA20 mutant N22A/H86K (ROWA) tetramer tetramer, 50 kDa Artificial protein (de … protein
Buffer:	20 mM HEPES, 150 mM NaCl, 5% glycerol,, pH: 7.5
Experiment:	SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Nov 30

Rational thermostabilisation of four-helix bundle dimeric de novo proteins. Sci Rep 11(1):7526 (2021)
Irumagawa S, Kobayashi K, Saito Y, Miyata T, Umetsu M, Kameda T, Arai R

R_g^Guinier	4.1	nm
D_max	18.1	nm
Volume^Porod	60	nm³

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