3IIU
Structure of the reconstituted Peridinin-Chlorophyll a-Protein (RFPCP) mutant N89L
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-10 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9334 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 68.510, 81.730, 75.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.070 - 1.450 |
R-factor | 0.15566 |
Rwork | 0.155 |
R-free | 0.17648 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3IIS RFPCP |
RMSD bond length | 0.017 |
RMSD bond angle | 3.295 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.070 | 1.550 |
High resolution limit [Å] | 1.450 | 1.450 |
Number of reflections | 37771 | |
<I/σ(I)> | 16.4 | 4.99 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 11.9 | 11.07 |
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 |