3L07
Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative bifunctional protein folD from Francisella tularensis.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-30 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.299, 73.385, 106.916 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.200 - 1.880 |
R-factor | 0.168 |
Rwork | 0.165 |
R-free | 0.20800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a4i |
RMSD bond length | 0.020 |
RMSD bond angle | 1.663 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.200 | 1.910 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.089 | 0.805 |
Number of reflections | 45729 | |
<I/σ(I)> | 9.4 | 2.78 |
Completeness [%] | 99.8 | 98.1 |
Redundancy | 7.2 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.2 M ammonium acetate, 0.1 M HEPES buffre, 25% PEG-3350, 10 mM NADP, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |