5UJW
Crystal structure of triosephosphate isomerase from Francisella tularensis subsp. tularensis SCHU S4
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 | 2013-12-12 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.97904 |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 76.724, 136.965, 84.602 |
| Unit cell angles | 90.00, 89.98, 90.00 |
Refinement procedure
| Resolution | 32.579 - 2.650 |
| R-factor | 0.2248 |
| Rwork | 0.216 |
| R-free | 0.25190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1TRE.pdb |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.569 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (dev_2650) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.700 |
| High resolution limit [Å] | 2.650 | 7.190 | 2.650 |
| Rmerge | 0.111 | 0.116 | 0.539 |
| Rmeas | 0.138 | 0.141 | 0.672 |
| Rpim | 0.081 | 0.079 | 0.399 |
| Total number of observations | 137054 | ||
| Number of reflections | 50936 | ||
| <I/σ(I)> | 7.4 | ||
| Completeness [%] | 98.8 | 91.2 | 99.5 |
| Redundancy | 2.7 | 2.8 | 2.7 |
| CC(1/2) | 0.946 | 0.590 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.1M Sodium Citrate, 10% PEG4000, 20% iso-propanol |
