Small Angle Scattering Biological Data Bank SASBDB

Browse by ORGANISM: other species

SASDSW7 – poly(GU) RNA with 12 GU repeats

polyGU RNA - (GU)12 experimental SAS data

Sample:	PolyGU RNA - (GU)12 monomer, 8 kDa synthetic RNA RNA
Buffer:	20 mM HEPES, 150 mM KCl, pH: 7
Experiment:	SAXS data collected at 12-ID-B, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Jun 10

Solution structure of poly(UG) RNA Journal of Molecular Biology :168340 (2023)
Escobar C, Petersen R, Tonelli M, Fan L, Henzler-Wildman K, Butcher S

R_g^Guinier	1.3	nm
D_max	4.7	nm
Volume^Porod	8	nm³

SASDSX8 – Solution scattering studies on 20 kDa accessory protein (P20) from Bacillus thuringiensis subsp. israelensis (ISPC-12)

20 kDa accessory protein experimental SAS data

Sample:	20 kDa accessory protein dimer, 42 kDa Bacillus thuringiensis serovar … protein
Buffer:	10 mM Tris, 100 mM NaCl, pH: 8
Experiment:	SAXS data collected at BL-18, INDUS-2 on 2023 Aug 15

20-kDa accessory protein (P20) from Bacillus thuringiensis subsp. israelensis ISPC-12: Purification, characterization, solution scattering and structural analysis International Journal of Biological Macromolecules :127985 (2023)
Kinkar O, Singh R, Prashar A, Kumar A, Hire R, Makde R

R_g^Guinier	3.0	nm
D_max	8.6	nm
Volume^Porod	67	nm³

SASDTX4 – G-actin - Skeletal muscle actin from Oryctolagus cuniculus: globular actin monomers

Actin, alpha skeletal muscle experimental SAS data

Sample:	Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer:	5 mM Tris/Tris-HCl, 0.1 mM CaCl2, 1 mM NaN3, 0.2 mM ATP, pH: 8.1
Experiment:	SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 1

Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I

R_g^Guinier	2.9	nm
D_max	8.5	nm
Volume^Porod	58	nm³

SASDTY4 – F-actin - Skeletal muscle actin from Oryctolagus cuniculus: fibrillar actin

Sample:	Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer:	5 mM Tris/Tris-HCl, 0.1 mM CaCl2, 1 mM NaN3, 1.0 mM ATP, 50 mM KCl, 2 mM MgCl2, pH: 8.1
Experiment:	SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 1

R_g^Guinier	15.7	nm
D_max	60.0	nm
Volume^Porod	4710	nm³

SASDTZ4 – I-actin - Skeletal muscle actin from Oryctolagus cuniculus: oligomer of time-inactivated actin (peak SEC fraction)

Sample:	Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer:	5 mM Tris/Tris-HCl, 2.0 mM EDTA, pH: 8.1
Experiment:	SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Nov 16

R_g^Guinier	4.9	nm
D_max	22.0	nm
Volume^Porod	549	nm³

SASDT25 – G- / I-actin mixture - Skeletal muscle actin from Oryctolagus cuniculus: mixture of globular actin monomers and inactivated actin monomers and dimers

Sample:	Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer:	5 mM Tris, 0.1 mM CaCl2, 1 mM NaN3, 0.2 mM ATP, pH: 8.1
Experiment:	SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 5

R_g^Guinier	3.1	nm
D_max	12.0	nm
Volume^Porod	84	nm³

SASDSH9 – SAXS data of Clostridium perfringens enterotoxin

Heat-labile enterotoxin B chain experimental SAS data

Sample:	Heat-labile enterotoxin B chain monomer, 36 kDa Clostridium perfringens protein
Buffer:	10 mM HEPES, 100 mM NaCl, 2% glycerol, pH: 7.4
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Nov 18

Structural Basis of Clostridium perfringens Enterotoxin Activation and Oligomerization by Trypsin Toxins 15(11):637 (2023)
Ogbu C, Kapoor S, Vecchio A

R_g^Guinier	2.7	nm
D_max	10.2	nm
Volume^Porod	46	nm³

SASDSJ9 – SAXS data of trypsinized Clostridium perfringens enterotoxin

Sample:	Heat-labile enterotoxin B chain monomer, 33 kDa Clostridium perfringens protein
Buffer:	10 mM HEPES, 100 mM NaCl, 2% glycerol, pH: 7.4
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Nov 18

Structural Basis of Clostridium perfringens Enterotoxin Activation and Oligomerization by Trypsin Toxins 15(11):637 (2023)
Ogbu C, Kapoor S, Vecchio A

R_g^Guinier	2.6	nm
D_max	9.5	nm
Volume^Porod	40	nm³

SASDQZ8 – Apoferritin (oligomeric mixtures) - reservoir sample storage with liquid jet delivery measured using XFEL

Ferritin light chain experimental SAS data

Sample:	Ferritin light chain 24-mer, 479 kDa Equus caballus protein
Buffer:	phosphate buffered saline, pH: 7.4
Experiment:	SANS data collected at SPB/SFX, European XFEL on 2021 May 14

Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS). Commun Biol 6(1):1057 (2023)
Blanchet CE, Round A, Mertens HDT, Ayyer K, Graewert M, Awel S, Franke D, Dörner K, Bajt S, Bean R, Custódio TF, de Wijn R, Juncheng E, Henkel A, Gruzinov A, Jeffries CM, Kim Y, Kirkwood H, Kloos M, Knoška J, Koliyadu J, Letrun R, Löw C, Makroczyova J, Mall A, Meijers R, Pena Murillo GE, Oberthür D, Round E, Seuring C, Sikorski M, Vagovic P, Valerio J, Wollweber T, Zhuang Y, Schulz J, Haas H, Chapman HN, Mancuso AP, Svergun D

R_g^Guinier

5.8

SASDQ39 – SARS-CoV-2 spike protein ACE2 receptor binding domain (RBD) - reservoir sample storage with liquid jet delivery measured using XFEL

Spike glycoprotein (ACE2 receptor binding domain) experimental SAS data

Spike glycoprotein (ACE2 receptor binding domain) Kratky plot

Sample:	Spike glycoprotein (ACE2 receptor binding domain) monomer, 29 kDa Severe acute respiratory … protein
Buffer:	phosphate buffered saline, pH: 7.4
Experiment:	SANS data collected at SPB/SFX, European XFEL on 2021 May 14

R_g^Guinier

3.0

First << Prev Page 52 of 220 Next >> Last