3TQ8
Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with trimethoprim
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4C |
Synchrotron site | NSLS |
Beamline | X4C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-08-09 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.340, 36.200, 53.810 |
Unit cell angles | 90.00, 110.27, 90.00 |
Refinement procedure
Resolution | 26.440 - 1.900 |
R-factor | 0.18479 |
Rwork | 0.182 |
R-free | 0.23715 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Unliganded CBU_1993 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.435 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.440 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 14597 | |
<I/σ(I)> | 15 | 8.8 |
Completeness [%] | 96.6 | 82.6 |
Redundancy | 4.6 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 100 mM HEPES, pH 7.5, 25% PEG 6000 , VAPOR DIFFUSION, SITTING DROP, temperature 298K |