1HTI
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.810, 75.390, 92.810 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.800 |
| R-factor | 0.167 |
| Rwork | 0.167 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 3.800 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.800 * |
| Rmerge | 0.055 * |
| Number of reflections | 9625 * |
| Completeness [%] | 85.5 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 4 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 4 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 100 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 20 (%) | |
| 4 | 1 | reservoir | 2-propanol | 10 (%) | |
| 5 | 1 | reservoir | dithiothreitol | 2 (mM) |






