SASBDB entries for UniProt ID:

SASDLZ9 – Streptococcus pneumoniae lipid II isoglutaminyl synthase MurT:GatD complex (no Zn2+)

UniProt ID: Q8DNZ9 (1-447) Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT

UniProt ID: Q8DNZ8 (None-None) Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTLipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD experimental SAS data
Streptococcus pneumoniae lipid II isoglutaminyl synthase MurT:GatD complex (no Zn2+) Rg histogram
Sample: Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT monomer, 52 kDa Streptococcus pneumoniae (strain … protein
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD monomer, 29 kDa Streptococcus pneumoniae (strain … protein
Buffer: 50 mM Hepes, 10 mM MgCl2, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jun 23
Unravelling the reaction mechanism of glutamate amidation in Staphylococcus aureus peptidoglycan PhD thesis, NOVA University Lisbon - (2022)
Francisco Miguel Piçarra Leisico, Mertens HD
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 126 nm3

SASDM22 – Staphylococcus aureus lipid II isoglutaminyl synthase MurT:GatD complex

UniProt ID: A0A0H2WZQ7 (2-437) Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT

UniProt ID: A0A0H2WZ38 (1-243) Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTLipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD experimental SAS data
Staphylococcus aureus lipid II isoglutaminyl synthase MurT:GatD complex Rg histogram
Sample: Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT monomer, 49 kDa Staphylococcus aureus (strain … protein
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD monomer, 28 kDa Staphylococcus aureus (strain … protein
Buffer: 100 mM Tris-HCl, 500 mM NaCl, 10 mM MgCl2, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Nov 29
Unravelling the reaction mechanism of glutamate amidation in Staphylococcus aureus peptidoglycan PhD thesis, NOVA University Lisbon - (2022)
Francisco Miguel Piçarra Leisico, Mertens HD
RgGuinier 3.1 nm
Dmax 10.5 nm
VolumePorod 121 nm3

SASDM42 – Cobalt/magnesium transport protein CorA in matched-out deuterated dodecylmaltoside (dDDM) micelles without Mg2+

UniProt ID: Q9WZ31 (1-351) Cobalt/magnesium transport protein CorA
Cobalt/magnesium transport protein CorA experimental SAS data
Cobalt/magnesium transport protein CorA Kratky plot
Sample: Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer: 20 mM Tris-DCl, 150 mM NaCl, 1 mM EDTA-NaOD, in 100% D2O, pH: 7.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23
Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation. Elife 11 (2022)
Johansen NT, Bonaccorsi M, Bengtsen T, Larsen AH, Tidemand FG, Pedersen MC, Huda P, Berndtsson J, Darwish T, Yepuri NR, Martel A, Pomorski TG, Bertarello A, Sansom M, Rapp M, Crehuet R, Schubeis T, Lindorff-Larsen K, Pintacuda G, Arleth L
RgGuinier 4.2 nm
Dmax 13.9 nm

SASDM52 – Cobalt/magnesium transport protein CorA in matched-out deuterated dodecylmaltoside (dDDM) micelles with bound Mg2+

UniProt ID: Q9WZ31 (1-351) Cobalt/magnesium transport protein CorA
Cobalt/magnesium transport protein CorA experimental SAS data
Cobalt/magnesium transport protein CorA Kratky plot
Sample: Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer: 20 mM Tris-DCl, 150 mM NaCl, 40 mM MgCl2, in 100% D2O, pH: 7.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23
Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation. Elife 11 (2022)
Johansen NT, Bonaccorsi M, Bengtsen T, Larsen AH, Tidemand FG, Pedersen MC, Huda P, Berndtsson J, Darwish T, Yepuri NR, Martel A, Pomorski TG, Bertarello A, Sansom M, Rapp M, Crehuet R, Schubeis T, Lindorff-Larsen K, Pintacuda G, Arleth L
RgGuinier 4.3 nm
Dmax 13.9 nm

SASDM62 – Cobalt/magnesium transport protein CorA in matched-out deuterated nanodiscs without Mg2+

UniProt ID: Q9WZ31 (1-351) Cobalt/magnesium transport protein CorA
Cobalt/magnesium transport protein CorA experimental SAS data
Cobalt/magnesium transport protein CorA Kratky plot
Sample: Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer: 20 mM Tris-DCl, 150 mM NaCl, 1 mM EDTA-NaOD, in 100% D2O, pH: 7.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23
Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation. Elife 11 (2022)
Johansen NT, Bonaccorsi M, Bengtsen T, Larsen AH, Tidemand FG, Pedersen MC, Huda P, Berndtsson J, Darwish T, Yepuri NR, Martel A, Pomorski TG, Bertarello A, Sansom M, Rapp M, Crehuet R, Schubeis T, Lindorff-Larsen K, Pintacuda G, Arleth L
RgGuinier 4.8 nm
Dmax 14.2 nm

SASDM72 – Cobalt/magnesium transport protein CorA in match-out deuterated nanodiscs with bound Mg2+

UniProt ID: Q9WZ31 (1-351) Cobalt/magnesium transport protein CorA
Cobalt/magnesium transport protein CorA experimental SAS data
Cobalt/magnesium transport protein CorA Kratky plot
Sample: Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer: 20 mM Tris-DCl, 150 mM NaCl, 40 mM MgCl2, in 100% D2O, pH: 7.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23
Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation. Elife 11 (2022)
Johansen NT, Bonaccorsi M, Bengtsen T, Larsen AH, Tidemand FG, Pedersen MC, Huda P, Berndtsson J, Darwish T, Yepuri NR, Martel A, Pomorski TG, Bertarello A, Sansom M, Rapp M, Crehuet R, Schubeis T, Lindorff-Larsen K, Pintacuda G, Arleth L
RgGuinier 4.9 nm
Dmax 14.3 nm

SASDMC2 – SWAXS data from Lysozyme Solution [Protein concentration 5 mg/ml] at 10 °C

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.3 nm
Dmax 4.2 nm

SASDMD2 – SWAXS data from Lysozyme Solution [Protein concentration 2.5 mg/ml] at 10 °C

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.3 nm

SASDME2 – SWAXS data from Lysozyme Solution [Protein concentration 1.8 mg/ml] at 10 °C

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.5 nm

SASDMF2 – SWAXS data from Lysozyme Solution [Protein concentration 0.9 mg/ml] at 10 °C

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 5.0 nm