5H8Z
Crystal structure of the C49A C353A mutant Fenna-Matthews-Olson Protein from Chlorobaculum Tepidum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-12-04 |
Detector | RAYONIX MX300-HS |
Wavelength(s) | 1.0 |
Spacegroup name | P 43 3 2 |
Unit cell lengths | 168.358, 168.358, 168.358 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.841 - 1.800 |
R-factor | 0.1602 |
Rwork | 0.159 |
R-free | 0.18900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eni |
RMSD bond length | 0.015 |
RMSD bond angle | 1.505 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.113 | 0.753 |
Number of reflections | 75406 | |
<I/σ(I)> | 63.9 | 6.4 |
Completeness [%] | 100.0 | |
Redundancy | 48.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | PEG 4000, 20% 2-proponal, sodium citrate, sodium chloride |