3AEQ
Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-10-14 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.632, 81.278, 177.103 |
Unit cell angles | 90.00, 100.43, 90.00 |
Refinement procedure
Resolution | 47.250 - 2.900 |
R-factor | 0.238 |
Rwork | 0.235 |
R-free | 0.29800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ZMP |
RMSD bond length | 0.010 |
RMSD bond angle | 1.347 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.900 |
Rmerge | 0.106 |
Number of reflections | 46513 |
Completeness [%] | 92.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | 16% PEG4000, 0.2M SODIUM/POTASSIUM PHOSPHATE(PH5.0), pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 277K |