3TQA
Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with NADPH
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 | 2010-10-28 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.419, 37.026, 52.989 |
Unit cell angles | 90.00, 108.02, 90.00 |
Refinement procedure
Resolution | 25.770 - 2.300 |
R-factor | 0.24965 |
Rwork | 0.247 |
R-free | 0.29854 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Unliganded CBU_1993 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.010 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
<I/σ(I)> | 20.2 | 1.7 |
Completeness [%] | 96.0 | 99.8 |
Redundancy | 5.7 | 5.8 |
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 |