Browse by MACROMOLECULE type: protein

SASDL67 – Mutation of the Active Site Residues of Thermus thermophilus 3‑Isopropylmalate Dehydrogenase

3-isopropylmalate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3-isopropylmalate dehydrogenase dimer, 73 kDa Thermus thermophilus protein
Buffer: 25 mM MOPS/NaOH, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Nov 16
Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure. Biochemistry 55(3):560-74 (2016)
Gráczer É, Szimler T, Garamszegi A, Konarev PV, Lábas A, Oláh J, Palló A, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M
RgGuinier 2.8 nm

SASDB44 – Aureochrome 1a from P. tricornutum, amino acids 148-378 (N-terminal truncation), dark state

Aureochrome 1a (N-terminally truncated) experimental SAS data
DAMMIN model
Sample: Aureochrome 1a (N-terminally truncated) dimer, 53 kDa Phaeodactylum tricornutum protein
Buffer: 20 mM HEPES 100 mM NaCl 10 mM MgCl2 5% w/v glycerol, pH: 7.5
Experiment: SAXS data collected at cSAXS, Swiss Light Source on 2015 Mar 11
Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence. Elife 5:e11860 (2016)
Heintz U, Schlichting I
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 90 nm3

SASDAJ8 – Light state solution structure of Aureochrome1a- A´α-LOV-Jα

Aureochrome1a-A´α-LOV-Jα experimental SAS data
DAMMIF model
Sample: Aureochrome1a-A´α-LOV-Jα dimer, 36 kDa Phaeodactylum tricornutum protein
Buffer: 10 mM Tris 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 16
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum. Structure 24(1):171-178 (2016)
Banerjee A, Herman E, Kottke T, Essen LO
RgGuinier 3.3 nm
Dmax 13.0 nm
VolumePorod 88 nm3

SASDAK8 – Dark state solution structure of Aureochrome1a- A´α-LOV-Jα

Aureochrome1a-A´α-LOV-Jα experimental SAS data
DAMMIF model
Sample: Aureochrome1a-A´α-LOV-Jα dimer, 36 kDa Phaeodactylum tricornutum protein
Buffer: 10 mM Tris 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 16
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum. Structure 24(1):171-178 (2016)
Banerjee A, Herman E, Kottke T, Essen LO
RgGuinier 3.2 nm
Dmax 13.0 nm
VolumePorod 67 nm3

SASDBD2 – Dark state solution structure of untagged Aureochrome1a- A´α-LOV-Jα

Aureochrome1a- A´α-LOV-Jα (Dark State) experimental SAS data
DAMMIN model
Sample: Aureochrome1a- A´α-LOV-Jα (Dark State) dimer, 32 kDa Phaeodactylum tricornutum protein
Buffer: 10 mM Tris-HCl, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 9
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum. Structure 24(1):171-178 (2016)
Banerjee A, Herman E, Kottke T, Essen LO
RgGuinier 2.7 nm
Dmax 9.2 nm
VolumePorod 58 nm3

SASDBE2 – Light state solution structure of untagged Aureochrome1a- A´α-LOV-Jα

Aureochrome1a- A´α-LOV-Jα (Light State) experimental SAS data
DAMMIN model
Sample: Aureochrome1a- A´α-LOV-Jα (Light State) dimer, 32 kDa Phaeodactylum tricornutum protein
Buffer: 10 mM Tris-HCl, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 9
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum. Structure 24(1):171-178 (2016)
Banerjee A, Herman E, Kottke T, Essen LO
RgGuinier 2.6 nm
Dmax 9.8 nm
VolumePorod 66 nm3

SASDB25 – Cardiac myosin binding protein-C: domains C5-C6-C7

Cardiac myosin binding protein-C: domains C5-C6-C7 experimental SAS data
Cardiac myosin binding protein-C: domains C5-C6-C7 Kratky plot
Sample: Cardiac myosin binding protein-C: domains C5-C6-C7 monomer, 36 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 250 mM NaCl, 2 mM TCEP, 0.02% sodium azide, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 18
Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects. Structure 24(1):105-115 (2016)
Nadvi NA, Michie KA, Kwan AH, Guss JM, Trewhella J
RgGuinier 3.8 nm
Dmax 14.1 nm
VolumePorod 55 nm3

SASDBY2 – Inorganic pyrophosphatase (PPase) from E. coli

Inorganic pyrophosphatase (PPase) from E. coli experimental SAS data
DAMMIN model
Sample: Inorganic pyrophosphatase (PPase) from E. coli hexamer, 117 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 166 nm3

SASDBZ2 – Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli

Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli experimental SAS data
DAMMIN model
Sample: Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli decamer, 381 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
Dmax 12.7 nm
VolumePorod 484 nm3

SASDB23 – 5-keto-4-deoxyuronate isomerase (KduI) from E. coli

5-keto-4-deoxyuronate isomerase (KduI) from E. coli experimental SAS data
NONE model
Sample: 5-keto-4-deoxyuronate isomerase (KduI) from E. coli None, Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.5 nm