|
|
|
Sample: |
Calredoxin, Redox protein from Chlamydomonas reinhardtii monomer, 40 kDa Chlamydomonas reinhardtii protein
|
Buffer: |
20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA, pH: 8 |
Experiment: |
SAXS
data collected at Rigaku BioSAXS-1000, Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University on 2015 Nov 17
|
Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii.
J Biol Chem (2019)
Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G
|
RgGuinier |
2.5 |
nm |
Dmax |
8.7 |
nm |
VolumePorod |
60 |
nm3 |
|
|
|
|
|
Sample: |
Calredoxin, Redox protein from Chlamydomonas reinhardtii monomer, 40 kDa Chlamydomonas reinhardtii protein
|
Buffer: |
20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM CaCl2, pH: 8 |
Experiment: |
SAXS
data collected at Rigaku BioSAXS-1000, Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University on 2015 Nov 17
|
Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii.
J Biol Chem (2019)
Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G
|
RgGuinier |
3.1 |
nm |
Dmax |
11.6 |
nm |
VolumePorod |
68 |
nm3 |
|
|
|
|
|
Sample: |
Human dystrophin central domain R8-15 fragment monomer, 100 kDa protein
|
Buffer: |
NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5 |
Experiment: |
SAXS
data collected at SWING, SOLEIL on 2015 Sep 23
|
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
|
RgGuinier |
10.1 |
nm |
Dmax |
36.0 |
nm |
|
|
|
|
|
Sample: |
Human dystrophin central domain R11-19 fragment monomer, 117 kDa protein
|
Buffer: |
NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5 |
Experiment: |
SAXS
data collected at SWING, SOLEIL on 2017 May 11
|
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
|
RgGuinier |
8.8 |
nm |
Dmax |
37.5 |
nm |
VolumePorod |
513 |
nm3 |
|
|
|
|
|
Sample: |
Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN repeats 2-15 dimer, 78 kDa Trypanosoma brucei protein
|
Buffer: |
20 mM Tris-HCl, 100 mM NaCl, pH: 7.5 |
Experiment: |
SAXS
data collected at BM29, ESRF on 2017 Jan 27
|
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.
PLoS One 15(12):e0242677 (2020)
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K
|
RgGuinier |
6.5 |
nm |
Dmax |
26.0 |
nm |
VolumePorod |
187 |
nm3 |
|
|
|
|
|
Sample: |
Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN (7-15) dimer, 52 kDa Trypanosoma brucei protein
|
Buffer: |
20 mM Tris-HCl, 200 mM NaCl, 2% (w/v) glycerol, 0.5 mM DTT, pH: 8.5 |
Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2016 Jun 11
|
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.
PLoS One 15(12):e0242677 (2020)
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K
|
RgGuinier |
4.1 |
nm |
Dmax |
15.5 |
nm |
VolumePorod |
56 |
nm3 |
|
|
|
|
|
Sample: |
Toxoplasma gondii Membrane Occupation and Recognition Nexus (MORN1) repeats 7-15 dimer, 49 kDa Toxoplasma gondii protein
|
Buffer: |
20 mM Tris-HCl, 100 mM NaCl, pH: 7.5 |
Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2016 Jun 10
|
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.
PLoS One 15(12):e0242677 (2020)
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K
|
RgGuinier |
4.0 |
nm |
Dmax |
17.0 |
nm |
VolumePorod |
55 |
nm3 |
|
|
|
|
|
Sample: |
MORN repeat-containing protein 1 dimer, 46 kDa Plasmodium falciparum protein
|
Buffer: |
20 mM Tris-HCl, 100 mM NaCl, pH: 7.5 |
Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2017 Dec 2
|
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.
PLoS One 15(12):e0242677 (2020)
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K
|
RgGuinier |
3.8 |
nm |
Dmax |
16.0 |
nm |
VolumePorod |
52 |
nm3 |
|
|
|
|
|
Sample: |
AGAP005335-PA monomer, 18 kDa Anopheles gambiae protein
AGAP005334-PA monomer, 18 kDa Anopheles gambiae protein
|
Buffer: |
500 mM NaCl, 20 mM CHES, 0.5 mM CaCl2, 1% glycerol, pH: 9 |
Experiment: |
SAXS
data collected at Rigaku BioSAXS-2000, Thomas Jefferson University on 2018 Aug 30
|
Solution structure, glycan specificity and of phenol oxidase inhibitory activity of Anopheles C-type lectins CTL4 and CTLMA2.
Sci Rep 9(1):15191 (2019)
Bishnoi R, Sousa GL, Contet A, Day CJ, Hou CD, Profitt LA, Singla D, Jennings MP, Valentine AM, Povelones M, Baxter RHG
|
RgGuinier |
2.5 |
nm |
Dmax |
8.0 |
nm |
VolumePorod |
58 |
nm3 |
|
|
|
|
|
Sample: |
12 base-paired RNA double helix monomer, 8 kDa RNA
|
Buffer: |
30 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7 |
Experiment: |
SAXS
data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
|
Salt Dependence of A-Form RNA Duplexes: Structures and Implications.
J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
|
|
|