Browse by DISSEMINATION: Published

SASDBJ4 – Wild-type LytA choline-binding domain

Lytic Amidase choline-binding domain experimental SAS data
SASREF model
Sample: Lytic Amidase choline-binding domain dimer, 17 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 150 mM NaCl 5 mM choline chloride 1 µM ZnCl2, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 11
Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae. MBio 5(1):e01120-13 (2014)
Mellroth P, Sandalova T, Kikhney A, Vilaplana F, Hesek D, Lee M, Mobashery S, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 3.3 nm
Dmax 10.0 nm
VolumePorod 49 nm3

SASDAR3 – PsrP functional binding region

Functional binding region (187-385) of the pneumococcal serine-rich repeat protein experimental SAS data
PsrP functional binding region Rg histogram
Sample: Functional binding region (187-385) of the pneumococcal serine-rich repeat protein monomer, 22 kDa Streptococcus pneumoniae protein
Buffer: 20 mM sodium citrate 250 mM NaCl 2.5 % Glycerol, pH: 5.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jul 2
The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold. Open Biol 4:130090 (2014)
Schulte T, Löfling J, Mikaelsson C, Kikhney A, Hentrich K, Diamante A, Ebel C, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 2.3 nm
Dmax 7.7 nm
VolumePorod 37 nm3

SASDH23 – Antigen 43 alpha domain

Alpha domain of Ag43a experimental SAS data
DAMMIN model
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2009 Nov 19
The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping. Proc Natl Acad Sci U S A 111(1):457-62 (2014)
Heras B, Totsika M, Peters KM, Paxman JJ, Gee CL, Jarrott RJ, Perugini MA, Whitten AE, Schembri MA
RgGuinier 3.6 nm
Dmax 12.2 nm
VolumePorod 62 nm3

SASDA35 – SeZinT-SeZnuA complex

High-affinity zinc transporter periplasmic componentZinc/cadmium-binding protein experimental SAS data
BUNCH model
Sample: High-affinity zinc transporter periplasmic component monomer, 33 kDa Salmonella enterica subsp. … protein
Zinc/cadmium-binding protein monomer, 23 kDa Salmonella enterica subsp. … protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 May 9
The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc. Biochim Biophys Acta 1840(1):535-44 (2014)
Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E
RgGuinier 2.5 nm
Dmax 8.5 nm
VolumePorod 55 nm3

SASDAX5 – Endophilin-CoA complex

Endophilin-A1 BAR domainarachidonyl-CoA experimental SAS data
SASREF model
Sample: Endophilin-A1 BAR domain dimer, 58 kDa Mus musculus protein
Arachidonyl-CoA, 60 kDa
Buffer: 50 mM TRIS-HCL 300 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Nov 27
Endophilin-A1 BAR domain interaction with arachidonyl CoA. Front Mol Biosci 1:20 (2014)
Petoukhov MV, Weissenhorn W, Svergun DI
RgGuinier 5.9 nm
Dmax 19.0 nm
VolumePorod 480 nm3

SASDAY5 – Free endophilin

Endophilin-A1 BAR domain experimental SAS data
CORAL model
Sample: Endophilin-A1 BAR domain dimer, 58 kDa Mus musculus protein
Buffer: 50 mM TRIS-HCL 300 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Feb 13
Endophilin-A1 BAR domain interaction with arachidonyl CoA. Front Mol Biosci 1:20 (2014)
Petoukhov MV, Weissenhorn W, Svergun DI
RgGuinier 3.3 nm
Dmax 13.5 nm
VolumePorod 90 nm3

SASDLT5 – Modification methylase SsoII (M.SsoII) protein bound to 12-bp DNA

Modification methylase SsoII12-bp DNA experimental SAS data
Modification methylase SsoII (M.SsoII) protein bound to 12-bp DNA Rg histogram
Sample: Modification methylase SsoII monomer, 43 kDa Shigella sonnei protein
12-bp DNA monomer, 8 kDa DNA
Buffer: 50 mM Na-phosphate buffer, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Mar 13
Flexibility of the linker between the domains of DNA methyltransferase SsoII revealed by small-angle X-ray scattering: implications for transcription regulation in SsoII restriction-modification system. PLoS One 9(4):e93453 (2014)
Konarev PV, Kachalova GS, Ryazanova AY, Kubareva EA, Karyagina AS, Bartunik HD, Svergun DI
RgGuinier 2.8 nm
Dmax 11.0 nm
VolumePorod 85 nm3

SASDB35 – Staphylococcus aureus thiaminase II

Thiaminase type II enzyme experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Thiaminase type II enzyme tetramer, 107 kDa Staphylococcus aureus protein
Buffer: 100 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 11
Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases. Acta Crystallogr D Biol Crystallogr 69(Pt 12):2320-9 (2013)
Begum A, Drebes J, Kikhney A, Müller IB, Perbandt M, Svergun D, Wrenger C, Betzel C
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 168 nm3

SASDMU2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.1 nm
Dmax 20.5 nm

SASDMV2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) monomer, 220 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 7.5 nm
Dmax 25.5 nm