2JK2
STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. CRYSTAL STRUCTURE OF THE WILD TYPE ENZYME.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-13 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.130, 73.060, 92.960 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 92.850 - 1.700 |
| R-factor | 0.222 |
| Rwork | 0.220 |
| R-free | 0.25200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wyi |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.153 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.050 | 0.300 |
| Number of reflections | 52549 | |
| <I/σ(I)> | 10.5 | 3 |
| Completeness [%] | 97.2 | 82.4 |
| Redundancy | 3.6 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 100 MM TRIS PH 8.5, 20% PEG MME2000, 10 MM NICL2 |
