SASDEQ9 – Cyclic GMP-AMP synthase (cGAS) with cyclic guanosine monophosphate–adenosine monophosphate (2'3'-cGAMP)

Cyclic GMP-AMP synthase2'-O,5'-O-((adenosine-3'-O,5'-O-diyl)bisphosphinico)guanosine experimental SAS data
Cyclic GMP-AMP synthase (cGAS) with cyclic guanosine monophosphate–adenosine monophosphate (2'3'-cGAMP) Rg histogram
Sample: Cyclic GMP-AMP synthase dimer, 123 kDa Homo sapiens protein
2'-O,5'-O-((adenosine-3'-O,5'-O-diyl)bisphosphinico)guanosine dimer, 1 kDa
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Apr 25
cGAS facilitates sensing of extracellular cyclic dinucleotides to activate innate immunity. EMBO Rep (2019)
Liu H, Moura-Alves P, Pei G, Mollenkopf HJ, Hurwitz R, Wu X, Wang F, Liu S, Ma M, Fei Y, Zhu C, Koehler AB, Oberbeck-Mueller D, Hahnke K, Klemm M, Guhlich-Bornhof U, Ge B, Tuukkanen A, Kolbe M, Dorhoi...
RgGuinier 3.9 nm
Dmax 14.1 nm
VolumePorod 127 nm3

SASDET9 – Gliding motility protein MglB: A GAP of Myxococcus xanthus MglA

Gliding motility protein MglB experimental SAS data
GASBOR model
Sample: Gliding motility protein MglB dimer, 34 kDa Myxococcus xanthus protein
Buffer: 150 mM NaCl, 1 mM DTT, 20 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Oct 9
MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus. Nat Commun 10(1):5300 (2019)
Galicia C, Lhospice S, Varela PF, Trapani S, Zhang W, Navaza J, Herrou J, Mignot T, Cherfils J
RgGuinier 2.8 nm
Dmax 10.3 nm
VolumePorod 56 nm3

SASDE37 – Lysine-specific demethylase 5B, KDM5B, in HEPES buffer

Lysine-specific demethylase 5B experimental SAS data
DAMFILT model
Sample: Lysine-specific demethylase 5B monomer, 176 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 300 mM NaCl, 5% (v/v) glycerol, 1mM DTT, pH: 7.7
Experiment: SAXS data collected at Xenocs BioXolver L with GeniX3D, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Oct 24
Molecular architecture of the Jumonji C family histone demethylase KDM5B. Sci Rep 9(1):4019 (2019)
Dorosz J, Kristensen LH, Aduri NG, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M
RgGuinier 8.8 nm
Dmax 26.9 nm

SASDKN2 – Matrix protein from Newcastle disease virus at neutral pH

Matrix protein experimental SAS data
DAMMIN model
Sample: Matrix protein , 40 kDa Newcastle disease virus … protein
Buffer: STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A
RgGuinier 3.5 nm

SASDKP2 – Matrix protein from Newcastle disease virus at acidic pH

Matrix protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Matrix protein dimer, 79 kDa Newcastle disease virus … protein
Buffer: STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A
RgGuinier 3.3 nm

SASDC28 – Mature α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) trimer, 81 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2014 Mar 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 2.8 nm
Dmax 8.7 nm
VolumePorod 913 nm3

SASDC38 – Truncated α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 275 nm3

SASDEK4 – C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data
DAMFILT model
Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
RgGuinier 1.7 nm
Dmax 5.4 nm
VolumePorod 22200 nm3

SASDEQ4 – Deletion mutant of the suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Deletion mutant of PmScsC experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Deletion mutant of PmScsC , 23 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 54 nm3

SASDER4 – Wild-type suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Suppressor of Copper Sensitivity C protein experimental SAS data
OTHER model
Sample: Suppressor of Copper Sensitivity C protein trimer, 74 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
RgGuinier 3.7 nm
Dmax 11.1 nm
VolumePorod 101 nm3

4101 hits found.