1AG1
MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | ELLIOTT GX-21 |
| Temperature [K] | 298 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1990-03 |
| Detector | ENRAF-NONIUS FAST |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 112.840, 97.600, 46.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.360 |
| R-factor | 0.15 * |
| Rwork | 0.150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6tim |
| RMSD bond length | 0.010 |
| RMSD bond angle | 3.000 |
| Data reduction software | MADNES |
| Data scaling software | BIOMOL |
| Phasing software | ISOMORPHOUS |
| Refinement software | TNT (5C) |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.360 |
| Rmerge | 0.063 |
| Number of reflections | 17592 |
| Completeness [%] | 87.5 |
| Redundancy | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 | Wierenga, R.K., (1984) J. Mol. Biol., 178, 487. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | triosephosphate isomerase | 4.5 (mg/ml) | |
| 2 | 1 | drop | ammonium sulfate | 60 (%) | |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | drop | MOPS | 0.2 (M) | |
| 5 | 1 | drop | dithiothreitol | 1 (mM) | |
| 6 | 1 | drop | sodium azide | 1 (mM) | |
| 7 | 1 | reservoir | ammonium sulphate | 60 (%) | |
| 8 | 1 | drop | ammonium sulphate | 0.9 (M) |
