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 |