3IT0
Crystal Structure Francisella tularensis histidine acid phosphatase complexed with phosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-17 |
| Detector | NOIR-1 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 41 |
| Unit cell lengths | 61.640, 61.640, 211.320 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.857 - 1.692 |
| R-factor | 0.191 |
| Rwork | 0.189 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3it1 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.905 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | PHENIX |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.950 | 1.760 |
| High resolution limit [Å] | 1.692 | 1.692 |
| Rmerge | 0.095 | 0.249 |
| Total number of observations | 26011 | |
| Number of reflections | 86186 | |
| <I/σ(I)> | 8.4 | 2.9 |
| Completeness [%] | 99.0 | 95.1 |
| Redundancy | 4.08 | 3.12 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 0.05 - 0.20 M Bis-Tris buffer pH 5.0 - 6.5, 17 -25 % PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
