1BGX
TAQ POLYMERASE IN COMPLEX WITH TP7, AN INHIBITORY FAB
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | SIEMENS |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1997-10 |
| Detector | SIEMENS |
| Spacegroup name | P 1 |
| Unit cell lengths | 76.600, 89.100, 89.300 |
| Unit cell angles | 100.70, 115.30, 95.30 |
Refinement procedure
| Resolution | 8.000 - 2.300 |
| R-factor | 0.189 |
| Rwork | 0.189 |
| R-free | 0.25300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1AYL AND 1TAQ |
| RMSD bond length | 0.010 |
| RMSD bond angle | 19.100 * |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | X-PLOR (3.8) |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.700 | 2.500 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.074 | 0.122 |
| Total number of observations | 414722 * | |
| Number of reflections | 81111 | |
| <I/σ(I)> | 8.2 | 8 |
| Completeness [%] | 82.0 | 75.9 |
| Redundancy | 5.1 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 20 * | PROTEIN WAS CRYSTALLIZED FROM 22% PEG 3350, 200 MM TRIS/HCL, PH 7.4. COMPLEX WAS MADE AT A PROTEIN CONCENTRATION OF 0.5 MG/ML, LEFT FOR 2-3 DAYS AT 4 DEGREES CELSIUS, CONCENTRATED TO 5MG/ML PROTEIN AND CRYSTALLIZATION CARRIED OUT IN HANGING DROPS., vapor diffusion - hanging drop, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | reservoir | PEG3350 | 22 (%) | |
| 3 | 1 | reservoir | Tris-HCl | 200 (mM) | pH7.4 |
| 4 | 1 | reservoir | 0.1 (%) |
