Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: No model

SASDAZ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data

DNA mismatch repair protein MutS Kratky plot

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK

R_g^Guinier

8.0

SASDA24 – MutS tetramer

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier	7.8	nm
D_max	27.0	nm

SASDAF4 – DmMfe2

Peroxisomal multifunctional enzyme type 2 experimental SAS data

Peroxisomal multifunctional enzyme type 2 Kratky plot

Sample:	Peroxisomal multifunctional enzyme type 2 dimer, 128 kDa Drosophila melanogaster protein
Buffer:	20 mM Sodium Phosphate 200 mM NaCl 5% (v/v) Glycerol 1mM Na2EDTA 1 mM NaN3, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 12

Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering. FEBS Lett 587(4):305-10 (2013)
Mehtälä ML, Haataja TJ, Blanchet CE, Hiltunen JK, Svergun DI, Glumoff T

R_g^Guinier	3.6	nm
D_max	12.0	nm

SASDAG4 – HsMfe2

Sample:	Peroxisomal multifunctional enzyme type 2 dimer, 159 kDa Homo sapiens protein
Buffer:	20 mM Sodium Phosphate 200 mM NaCl 5% (v/v) Glycerol 1mM Na2EDTA 1 mM NaN3, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 22

R_g^Guinier	4.6	nm
D_max	15.0	nm

SASDAV4 – uPAR wild-type AE105 complex

Urokinase plasminogen activator surface receptorsynthetic peptide AE105 experimental SAS data

Urokinase plasminogen activator surface receptor synthetic peptide AE105 Kratky plot

Sample:	Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein Synthetic peptide AE105 monomer, 1 kDa protein
Buffer:	25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 10

A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). J Biol Chem 287(41):34304-15 (2012)
Mertens HD, Kjaergaard M, Mysling S, Gårdsvoll H, Jørgensen TJ, Svergun DI, Ploug M

R_g^Guinier	2.5	nm
D_max	8.5	nm
Volume^Porod	61	nm³

SASDAW4 – uPAR wild-type AE234 complex

Urokinase plasminogen activator surface receptorsynthetic peptide AE234 experimental SAS data

Urokinase plasminogen activator surface receptor synthetic peptide AE234 Kratky plot

Sample:	Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein Synthetic peptide AE234 monomer, 1 kDa protein
Buffer:	25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 10

R_g^Guinier	2.4	nm
D_max	8.3	nm
Volume^Porod	57	nm³

SASDAX4 – uPAR wild-type ATF complex

Urokinase plasminogen activator surface receptorUrokinase-type plasminogen activator experimental SAS data

Urokinase plasminogen activator surface receptor Urokinase-type plasminogen activator Kratky plot

Sample:	Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein Urokinase-type plasminogen activator monomer, 49 kDa Homo sapiens protein
Buffer:	25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 10

R_g^Guinier	2.8	nm
D_max	9.4	nm
Volume^Porod	102	nm³

SASDNN2 – Experimental SAXS data for hemoglobin conjucted with six-seven copies of PEG dimer (Hb2) at concentration c = 21 mg/ml

Human hemoglobin conjugated with six-seven copies of 5-kDa PEG experimental SAS data

Human hemoglobin conjugated with six-seven copies of 5-kDa PEG Kratky plot

Sample:	Human hemoglobin conjugated with six-seven copies of 5-kDa PEG dimer, 62 kDa Homo sapiens protein
Buffer:	Ringer's lactate solution, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 19

Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R

R_g^Guinier

3.0

SASDNQ2 – Experimental SAXS data for hemoglobin conjucted with two copies of PEG dimer (Hb2) at concentration c = 25 mg/ml

Human hemoglobin conjugated with two copies of 5-kDa PEG experimental SAS data

Human hemoglobin conjugated with two copies of 5-kDa PEG Kratky plot

Sample:	Human hemoglobin conjugated with two copies of 5-kDa PEG dimer, 62 kDa Homo sapiens protein
Buffer:	Ringer's lactate solution, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 19

R_g^Guinier

2.4

SASDNT2 – Experimental SAXS data for native hemoglobin (Hb) at concentration c = 31.25 mg/ml

Hemoglobin subunit alphaHemoglobin subunit beta experimental SAS data

Hemoglobin subunit alpha Hemoglobin subunit beta Kratky plot

Sample:	Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Buffer:	Ringer's lactate solution, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 19

R_g^Guinier

2.2

First << Prev Page 223 of 224 Next >> Last