Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Hybrid

SASDFW7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆328-352 (MCoA∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) experimental SAS data

Sample:	Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer:	50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2017 Jul 13

The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L

R_g^Guinier	2.3	nm
D_max	6.9	nm
Volume^Porod	77	nm³

SASDFX7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆337-346 (MCoA∆337-346)

Aquifex aeolicus McoA metaloxidase ∆337-346 experimental SAS data

Sample:	Aquifex aeolicus McoA metaloxidase ∆337-346 monomer, 54 kDa Aquifex aeolicus protein
Buffer:	50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Dec 4

R_g^Guinier	2.3	nm
D_max	7.0	nm
Volume^Porod	78	nm³

SASDFY7 – Aquifex aeolicus McoA metaloxidase

Aquifex aeolicus McoA metaloxidase experimental SAS data

Sample:	Aquifex aeolicus McoA metaloxidase monomer, 55 kDa Aquifex aeolicus protein
Buffer:	50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Apr 15

R_g^Guinier	2.3	nm
D_max	7.5	nm
Volume^Porod	79	nm³

SASDH92 – Plasmodium falciparum lipocalin (PF3D7_0925900): Dimer-tetramer equilibrium through a concentration series (combined batch and SEC-SAXS measurements)

Plasmodium falciparum Lipocalin experimental SAS data

Sample:	Plasmodium falciparum Lipocalin tetramer, 89 kDa Plasmodium falciparum protein
Buffer:	20 mM Tris pH7.5, 150 mM NaCl, 5% v/v glycerol, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 Apr 8

Structure-Based Identification and Functional Characterization of a Lipocalin in the Malaria Parasite Plasmodium falciparum Cell Reports 31(12):107817 (2020)
Burda P, Crosskey T, Lauk K, Zurborg A, Söhnchen C, Liffner B, Wilcke L, Pietsch E, Strauss J, Jeffries C, Svergun D, Wilson D, Wilmanns M, Gilberger T

R_g^Guinier	3.2	nm
D_max	10.3	nm
Volume^Porod	126	nm³

SASDG37 – 1:2 heterotrimer of pUL7 and pUL51(8-142) from herpes simplex virus 1

Tegument protein UL7Tegument protein UL51 experimental SAS data

Sample:	Tegument protein UL7 monomer, 34 kDa Human alphaherpesvirus 1 … protein Tegument protein UL51 dimer, 30 kDa Human alphaherpesvirus 1 … protein
Buffer:	20 mM tris, 200 mM NaCl, 3% (v/v) glycerol, 0.25 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 16

Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex. Elife 9 (2020)
Butt BG, Owen DJ, Jeffries CM, Ivanova L, Hill CH, Houghton JW, Ahmed MF, Antrobus R, Svergun DI, Welch JJ, Crump CM, Graham SC

R_g^Guinier	3.0	nm
D_max	11.5	nm
Volume^Porod	116	nm³

SASDHN8 – Human tumor necrosis factor receptor superfamily member 5 (CD40) extracellular domain in complex with human immunoglobulin gamma 1 (IgG1) 341G2 F(ab)

Tumor necrosis factor receptor superfamily member 5Human 341G2 F(ab) experimental SAS data

Sample:	Tumor necrosis factor receptor superfamily member 5 monomer, 19 kDa Homo sapiens protein Human 341G2 F(ab) monomer, 73 kDa Homo sapiens protein
Buffer:	Phosphate-buffered saline, pH: 7
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Sep 18

Isotype Switching Converts Anti-CD40 Antagonism to Agonism to Elicit Potent Antitumor Activity Cancer Cell (2020)
Yu X, Chan H, Fisher H, Penfold C, Kim J, Inzhelevskaya T, Mockridge C, French R, Duriez P, Douglas L, English V, Verbeek J, White A, Tews I, Glennie M, Cragg M

R_g^Guinier	3.7	nm
D_max	13.4	nm
Volume^Porod	97	nm³

SASDGG2 – Interleukin 11 receptor subunit alpha

Interleukin-11 receptor subunit alpha experimental SAS data

Sample:	Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Buffer:	20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8

The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement Journal of Biological Chemistry :jbc.RA119.012351 (2020)
Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M

R_g^Guinier	3.0	nm
D_max	9.5	nm
Volume^Porod	41	nm³

SASDGH2 – Interleukin 11, N-terminally truncated

Sample:	Interleukin 11 monomer, 18 kDa Homo sapiens protein
Buffer:	20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8

R_g^Guinier	1.7	nm
D_max	5.4	nm
Volume^Porod	22	nm³

SASDGJ2 – Interleukin 11, full length

Sample:	Interleukin 11 monomer, 19 kDa Homo sapiens protein
Buffer:	20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8

R_g^Guinier	1.9	nm
D_max	6.1	nm
Volume^Porod	28	nm³

SASDGK2 – Interleukin 11/Interleukin 11 receptor alpha complex

Interleukin-11 receptor subunit alphaInterleukin 11 experimental SAS data

Sample:	Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein Interleukin 11 monomer, 18 kDa Homo sapiens protein
Buffer:	20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8

R_g^Guinier	3.3	nm
D_max	10.2	nm
Volume^Porod	84	nm³

First << Prev Page 96 of 163 Next >> Last