4LRS
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-11 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 149.880, 92.210, 56.480 |
| Unit cell angles | 90.00, 100.59, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.550 |
| R-factor | 0.166 |
| Rwork | 0.164 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nvm |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.461 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.350 | 1.590 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.059 | 0.365 |
| Number of reflections | 424737 | |
| <I/σ(I)> | 13.68 | 3.06 |
| Completeness [%] | 97.6 | 85.2 |
| Redundancy | 3.98 | 3.01 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 26-34% PEG 4000 or 3350, 0.1 M Tris, 0.2 M Li2SO4, 0.005M NAD, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
