|
|
|
|
|
| Sample: |
Beta-amylase tetramer, 231 kDa Zea mays protein
|
| Buffer: |
50 mM HEPES, 25 mM NaCl, and 0.2 mM TCEP, pH: 7.5 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
|
The BAM7
gene in Zea mays
encodes a protein with similar structural and catalytic properties to Arabidopsis
BAM2
Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
|
| RgGuinier |
5.1 |
nm |
| Dmax |
13.9 |
nm |
| VolumePorod |
467 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
|
| Buffer: |
20 mM HEPES, 150 mM NaCl, and 0.2 mM TCEP, pH: 7.3 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
|
The BAM7
gene in Zea mays
encodes a protein with similar structural and catalytic properties to Arabidopsis
BAM2
Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
|
| RgGuinier |
4.4 |
nm |
| Dmax |
14.1 |
nm |
| VolumePorod |
296 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
|
| Buffer: |
20 mM Tris, 100 mM NaCl, pH: 7.7 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 4
|
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition
Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
|
| RgGuinier |
3.2 |
nm |
| Dmax |
9.1 |
nm |
| VolumePorod |
170 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
|
| Buffer: |
20 mM Tris, 100 mM NaCl, pH: 7.7 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
|
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition
Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
|
| RgGuinier |
3.1 |
nm |
| Dmax |
9.1 |
nm |
| VolumePorod |
165 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Citrate synthase, mitochondrial monomer, 3 kDa Homo sapiens protein
|
| Buffer: |
20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Nov 4
|
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition
Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
|
| RgGuinier |
3.1 |
nm |
| Dmax |
8.7 |
nm |
| VolumePorod |
165 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Amyloid-beta precursor protein monomer, 4 kDa Homo sapiens protein
|
| Buffer: |
20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
|
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition
Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
|
| RgGuinier |
3.0 |
nm |
| Dmax |
8.5 |
nm |
| VolumePorod |
175 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Dockerin domain-containing protein monomer, 26 kDa Ruminococcus bromii protein
|
| Buffer: |
phosphate buffered saline, 1 mM TCEP, pH: 7 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 14
|
Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome
Journal of Biological Chemistry :101896 (2022)
Cerqueira F, Photenhauer A, Doden H, Brown A, Abdel-Hamid A, Moraïs S, Bayer E, Wawrzak Z, Cann I, Ridlon J, Hopkins J, Koropatkin N
|
| RgGuinier |
2.0 |
nm |
| Dmax |
7.8 |
nm |
| VolumePorod |
45 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Dockerin domain-containing protein monomer, 26 kDa Ruminococcus bromii protein
|
| Buffer: |
phosphate buffered saline, 1 mM TCEP, pH: 7 |
| Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 14
|
Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome
Journal of Biological Chemistry :101896 (2022)
Cerqueira F, Photenhauer A, Doden H, Brown A, Abdel-Hamid A, Moraïs S, Bayer E, Wawrzak Z, Cann I, Ridlon J, Hopkins J, Koropatkin N
|
| RgGuinier |
5.2 |
nm |
| Dmax |
19.0 |
nm |
| VolumePorod |
84 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Roquin-1 monomer, 18 kDa Mus musculus protein
|
| Buffer: |
150 mM NaCl, 20 mM Tris, 2 mM TCEP, pH: 7 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2020 Jun 1
|
NMR-derived secondary structure of the full-length Ox40 mRNA 3'UTR and its multivalent binding to the immunoregulatory RBP Roquin.
Nucleic Acids Res (2022)
Tants JN, Becker LM, McNicoll F, Müller-McNicoll M, Schlundt A
|
| RgGuinier |
1.9 |
nm |
| Dmax |
7.0 |
nm |
| VolumePorod |
35 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Roquin-1 extROQ monomer, 35 kDa Mus musculus protein
|
| Buffer: |
150 mM NaCl, 20 mM Tris, 2 mM TCEP, pH: 7 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2020 Jun 1
|
NMR-derived secondary structure of the full-length Ox40 mRNA 3'UTR and its multivalent binding to the immunoregulatory RBP Roquin.
Nucleic Acids Res (2022)
Tants JN, Becker LM, McNicoll F, Müller-McNicoll M, Schlundt A
|
| RgGuinier |
2.8 |
nm |
| Dmax |
14.0 |
nm |
| VolumePorod |
53 |
nm3 |
|
|