1F3F
STRUCTURE OF THE H122G NUCLEOSIDE DIPHOSPHATE KINASE / D4T-TRIPHOSPHATE.MG COMPLEX
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE D41A |
| Synchrotron site | LURE |
| Beamline | D41A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 70.018, 70.018, 152.098 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.730 - 1.850 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| R-free | 0.23400 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 22.900 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.730 | 1.970 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.056 * | 0.328 |
| Number of reflections | 37405 * | |
| Completeness [%] | 99.3 * | 98.7 |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 | pH 7.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG400 | 19 (%) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | 20 (mM) | ||
| 4 | 1 | drop | protein | 6 (mg/ml) | |
| 5 | 1 | drop | d4T triphosphate | 7.5 (mM) | |
| 6 | 1 | reservoir | PEG400 | 38 (%) |
