3GQS
Crystal structure of the FHA domain of CT664 protein from Chlamydia trachomatis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-11-19 |
Detector | SBC-3 |
Wavelength(s) | 0.9794 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 49.387, 86.475, 94.592 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 31.770 - 2.200 |
R-factor | 0.19675 |
Rwork | 0.194 |
R-free | 0.24419 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ff4 |
RMSD bond length | 0.020 |
RMSD bond angle | 1.636 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.5.0062) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.770 | 2.050 |
High resolution limit [Å] | 2.020 | 2.020 |
Rmerge | 0.529 | |
Number of reflections | 13892 | |
<I/σ(I)> | 24.379 | 1.3 |
Completeness [%] | 98.3 | 89 |
Redundancy | 6.9 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 0.2M Na di-Hydrogen phosphate, 20% PEG 3350, VAPOR DIFFUSION, temperature 293K |