3AGA
Crystal structure of RCC-bound red chlorophyll catabolite reductase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-06-28 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.500, 85.640, 133.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.960 - 2.600 |
R-factor | 0.23 |
Rwork | 0.228 |
R-free | 0.29900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zxl |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 16060 | |
<I/σ(I)> | 12.3 | 1.8 |
Completeness [%] | 96.8 | 91.9 |
Redundancy | 7 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 30% PEG 2000 monomethyl ether, 0.1M ammonium acetate, 3% dioxane, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |