Browse by MODEL: Ab initio only

SASDHK3 – Braveheart RNA + Cellular nucleic acid-binding protein (CNBP)

Braveheart RNACellular nucleic acid-binding protein experimental SAS data
DAMMIN model
Sample: Braveheart RNA monomer, 205 kDa Homo sapiens RNA
Cellular nucleic acid-binding protein monomer, 22 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 9.8 nm
Dmax 30.2 nm
VolumePorod 1660 nm3

SASDHL3 – Braveheart Fragment 1 + Cellular nucleic acid-binding protein (CNBP)

Cellular nucleic acid-binding proteinBraveheart Fragment 1 experimental SAS data
DAMMIN model
Sample: Cellular nucleic acid-binding protein monomer, 22 kDa Homo sapiens protein
Braveheart Fragment 1 monomer, 116 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 8.2 nm
Dmax 27.0 nm
VolumePorod 455 nm3

SASDG95 – Phosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex

Resistance to inhibitors of cholinesterase 8 homolog AGuanine nucleotide-binding protein G(i) subunit alpha-1 experimental SAS data
DAMMIF model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Rattus norvegicus protein
Guanine nucleotide-binding protein G(i) subunit alpha-1 monomer, 38 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 30
Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1 Nature Communications 11(1) (2020)
McClelland L, Zhang K, Mou T, Johnston J, Yates-Hansen C, Li S, Thomas C, Doukov T, Triest S, Wohlkonig A, Tall G, Steyaert J, Chiu W, Sprang S
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 120 nm3

SASDEN3 – Perivitellin PmPV2

P. maculata perivitellin 2 experimental SAS data
DAMMIN model
Sample: P. maculata perivitellin 2 dimer, 188 kDa Pomacea maculata protein
Buffer: 20 mM Tris, pH: 7
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 Mar 26
Exaptation of two ancient immune proteins into a new dimeric pore-forming toxin in snails. J Struct Biol 211(2):107531 (2020)
Giglio ML, Ituarte S, Milesi V, Dreon MS, Brola TR, Caramelo J, Ip JCH, Maté S, Qiu JW, Otero LH, Heras H
RgGuinier 4.4 nm
Dmax 14.3 nm
VolumePorod 267 nm3

SASDDG3 – Solution Structure of Archaeal Biofilm Regulator 2 (AbfR2) in Complex with DNA

Sa0446 binding sequence 40bpTranscriptional regulator Lrs14-like protein experimental SAS data
DAMMIF model
Sample: Sa0446 binding sequence 40bp monomer, 25 kDa DNA
Transcriptional regulator Lrs14-like protein dimer, 33 kDa Sulfolobus acidocaldarius protein
Buffer: 300 mM NaCl, 20 mM HEPES, pH 7.5, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 5
Solution Structure of Archaeal Biofilm Regulator 2 (AbfR2) in Complex with 40 bp DNA
Marian Vogt
RgGuinier 3.4 nm
Dmax 12.8 nm
VolumePorod 60 nm3

SASDE52 – Ribonuclease E from Escherichia coli

Endoribonuclease E experimental SAS data
DAMFILT model
Sample: Endoribonuclease E tetramer, 247 kDa Escherichia coli protein
Buffer: 10 mM DTT, 10 mM MgCl2, 0.5 M NaCl, 20 mM Tris, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Feb 11
A structural and biochemical comparison of Ribonuclease E homologues from pathogenic bacteria highlights species-specific properties. Sci Rep 9(1):7952 (2019)
Mardle CE, Shakespeare TJ, Butt LE, Goddard LR, Gowers DM, Atkins HS, Vincent HA, Callaghan AJ
RgGuinier 5.0 nm
Dmax 16.1 nm
VolumePorod 468 nm3

SASDF96 – Olfactomedin-1 BMY isoform

Noelin experimental SAS data
DAMMIF model
Sample: Noelin tetramer, 72 kDa Mus musculus protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 5
Design and structural characterisation of olfactomedin-1 variants as tools for functional studies. BMC Mol Cell Biol 20(1):50 (2019)
Pronker MF, van den Hoek H, Janssen BJC
RgGuinier 5.4 nm
Dmax 16.3 nm
VolumePorod 160 nm3

SASDFU4 – Conformation of R11-15 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 6.2 nm
Dmax 28.1 nm
VolumePorod 144 nm3

SASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 8.1 nm
Dmax 29.6 nm
VolumePorod 231 nm3

SASDGV6 – Cysteine synthase A

Cysteine synthase A experimental SAS data
DAMMIN model
Sample: Cysteine synthase A dimer, 71 kDa Escherichia coli protein
Buffer: 20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE, pH: 7.5
Experiment: SAXS data collected at Austrian SAXS beamline 5.2L, ELETTRA on 2016 Jun 1
Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action. Int J Mol Sci 20(20) (2019)
Rosa B, Marchetti M, Paredi G, Amenitsch H, Franko N, Benoni R, Giabbai B, De Marino MG, Mozzarelli A, Ronda L, Storici P, Campanini B, Bettati S
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 108 nm3