4POC
Structure of Triosephosphate Isomerase Wild Type human enzyme.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-03-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.920, 48.851, 93.966 |
| Unit cell angles | 90.00, 103.66, 90.00 |
Refinement procedure
| Resolution | 46.564 - 1.601 |
| R-factor | 0.1548 |
| Rwork | 0.153 |
| R-free | 0.18730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2jk2 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.962 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 4.340 | 1.600 |
| Rmerge | 0.077 | 0.071 | 0.442 |
| Number of reflections | 52380 | ||
| <I/σ(I)> | 11.3 | ||
| Completeness [%] | 93.8 | 98.6 | 54.2 |
| Redundancy | 5.6 | 5.1 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 35% PEG 2000 MME, 0.05 KBr, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
