1TN8
Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-01-13 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 61 |
| Unit cell lengths | 171.147, 171.147, 69.326 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.060 - 2.250 |
| R-factor | 0.193 |
| Rwork | 0.193 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1d8d |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Number of reflections | 55180 | |
| <I/σ(I)> | 14.7 | 2.5 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 6.5 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 290 | 14% PEG 8000, 600 mM ammonium acetate pH 5.7, 20 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
