2VOM
Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 113 |
| Detector technology | CCD |
| Collection date | 2007-11-20 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 320.521, 47.288, 68.957 |
| Unit cell angles | 90.00, 97.20, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.850 |
| R-factor | 0.2194 |
| Rwork | 0.219 |
| R-free | 0.25250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wyi |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.251 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.200 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.130 | 0.390 |
| Number of reflections | 81960 | |
| <I/σ(I)> | 9.6 | 3.3 |
| Completeness [%] | 93.0 | 93 |
| Redundancy | 3.4 | 3.57 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 100 MM TRIS PH 8.5, 20% PEG MME2000, 4% POLYPROPYLENE GLYCOL P400, 10 MM NICL2 |
