Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery.
Bogner AN,
Ji J,
Tanner JJ
Protein Eng Des Sel
(2022 Nov 30)
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Sample: |
Minimal proline dehydrogenase domain of proline utilization A (design #2) dimer, 87 kDa Sinorhizobium meliloti protein
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Buffer: |
25 mM HEPES pH 7.6, 150 mM NaCl, and 1mM TCEP, pH: 7.6 |
Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2022 Apr 12
|
|
RgGuinier |
2.7 |
nm |
Dmax |
9.5 |
nm |
VolumePorod |
102 |
nm3 |
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|
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|
Sample: |
Minimal proline dehydrogenase domain of proline utilization A (design #2) dimer, 87 kDa Sinorhizobium meliloti protein
|
Buffer: |
25 mM HEPES pH 7.6, 150 mM NaCl, and 1mM TCEP, pH: 7.6 |
Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2022 Apr 12
|
|
RgGuinier |
2.9 |
nm |
Dmax |
9.7 |
nm |
VolumePorod |
102 |
nm3 |
|
|
|
|
|
Sample: |
Minimal proline dehydrogenase domain of proline utilization A (design #2) dimer, 87 kDa Sinorhizobium meliloti protein
|
Buffer: |
25 mM HEPES pH 7.6, 150 mM NaCl, and 1mM TCEP, pH: 7.6 |
Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2022 Apr 12
|
|
RgGuinier |
3.0 |
nm |
Dmax |
9.8 |
nm |
VolumePorod |
108 |
nm3 |
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