4LRT
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 |
| Wavelength(s) | 0.8856 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 94.500, 116.700, 131.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.450 - 1.500 |
| R-factor | 0.15234 |
| Rwork | 0.151 |
| R-free | 0.17016 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4lrs |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.334 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.450 | 1.540 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.033 | 0.428 |
| Number of reflections | 812171 | |
| <I/σ(I)> | 22.53 | 3.04 |
| Completeness [%] | 90.0 | 52.5 |
| Redundancy | 3.89 | 3.15 |
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, 0.005 M CoA, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
