1FT1
CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 96 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-06-17 |
| Detector | RIGAKU |
| Spacegroup name | P 65 |
| Unit cell lengths | 167.060, 167.060, 97.900 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.250 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.26000 |
| Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 20.436 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.280 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.049 | 0.556 |
| Total number of observations | 442035 * | |
| Number of reflections | 72290 | |
| <I/σ(I)> | 18.4 | 0.92 |
| Completeness [%] | 98.1 | 81.8 |
| Redundancy | 4 | 1.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 17 * | HANG DROP, PROTEIN CONCENTRATION BETWEEN 4 AND 16MG/ML IN 20 MM KCL, 10MM ZNCL, 10MM DTT, 20MM TRIS PH7.7, RESERVOIR SOLUTION OF 13 - 18% PEG 8000, 200MM AMMONIUM ACETATE, PH 7.0, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | FTase | 4-16 (mg/ml) | |
| 2 | 1 | drop | 20 (mM) | ||
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 10 (mM) | |
| 5 | 1 | drop | Tris-HCl | 20 (mM) | |
| 6 | 1 | drop | PEG8000 | 13-15 (%(w/v)) | |
| 7 | 1 | drop | ammonium acetate | 200 (mM) | |
| 8 | 1 | reservoir | PEG8000 | 13-15 (%(w/v)) | |
| 9 | 1 | reservoir | ammonium acetate | 200 (mM) |
