2X21
Structure of Peridinin-Chlorophyll-Protein reconstituted with BChl-a
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-02 |
Detector | ADSC CCD |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 68.490, 81.810, 74.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.010 - 1.750 |
R-factor | 0.148 |
Rwork | 0.146 |
R-free | 0.18600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3iis |
RMSD bond length | 0.032 |
RMSD bond angle | 3.711 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.010 | 1.800 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.090 | 0.530 |
Number of reflections | 21555 | |
<I/σ(I)> | 14.6 | 3.1 |
Completeness [%] | 99.7 | 99.8 |
Redundancy | 4.8 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 296 | 0.1M CDCL2, 0,1M SODIUM ACETATE PH 4.6, 20-24% PEG 400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K |