3AGC
F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-13 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.089, 84.321, 131.518 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.21181 |
Rwork | 0.209 |
R-free | 0.26992 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zxl |
RMSD bond length | 0.008 |
RMSD bond angle | 1.526 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 34491 | |
<I/σ(I)> | 10.6 | 8 |
Completeness [%] | 99.6 | 100 |
Redundancy | 5.9 | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 35% PEG 2000 monomethyl ether, 0.1M ammonium acetate, 3% dioxane, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |