|
|
|
|
|
| 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: |
Dehydrodolichyl diphosphate synthase complex subunit DHDDS dimer, 78 kDa Homo sapiens protein
|
| Buffer: |
Tris-HCl, 150 mM NaCl, 20 mM 2-mercaptoethanol and 0.02% Triton-X100, pH: 7.5
|
| Experiment: |
SAXS
data collected at BM29, ESRF on 2018 May 2
|
Structural Characterization of Full-Length Human Dehydrodolichyl Diphosphate Synthase Using an Integrative Computational and Experimental Approach.
Biomolecules 9(11) (2019)
Lisnyansky Bar-El M, Lee SY, Ki AY, Kapelushnik N, Loewenstein A, Chung KY, Schneidman-Duhovny D, Giladi M, Newman H, Haitin Y
|
| RgGuinier |
3.2 |
nm |
| Dmax |
13.0 |
nm |
| VolumePorod |
122 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
|
| Buffer: |
50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
|
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1
|
Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.
J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ
|
| RgGuinier |
3.8 |
nm |
| Dmax |
11.5 |
nm |
| VolumePorod |
350 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
|
| Buffer: |
50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
|
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1
|
Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.
J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ
|
| RgGuinier |
3.8 |
nm |
| Dmax |
10.7 |
nm |
| VolumePorod |
326 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
|
| Buffer: |
50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
|
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1
|
Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.
J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ
|
| RgGuinier |
3.8 |
nm |
| Dmax |
10.7 |
nm |
| VolumePorod |
315 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Alpha-aminoadipic semialdehyde dehydrogenase E399Q , 56 kDa Homo sapiens protein
|
| Buffer: |
50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
|
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1
|
Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.
J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ
|
| RgGuinier |
3.7 |
nm |
| Dmax |
10.3 |
nm |
| VolumePorod |
237 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Alpha-aminoadipic semialdehyde dehydrogenase E399Q , 56 kDa Homo sapiens protein
|
| Buffer: |
50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
|
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1
|
Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.
J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ
|
| RgGuinier |
3.8 |
nm |
| Dmax |
10.8 |
nm |
| VolumePorod |
238 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Alpha-aminoadipic semialdehyde dehydrogenase E399Q , 56 kDa Homo sapiens protein
|
| Buffer: |
50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH: 8
|
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 1
|
Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.
J Inherit Metab Dis (2019)
Laciak AR, Korasick DA, Gates KS, Tanner JJ
|
| RgGuinier |
3.8 |
nm |
| Dmax |
10.6 |
nm |
| VolumePorod |
255 |
nm3 |
|
|
