1MZC
Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldiphosphate and Inhibitor Compound 33a
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-02-17 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 61 |
| Unit cell lengths | 178.385, 178.385, 64.579 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.000 * - 2.000 |
| R-factor | 0.177 |
| Rwork | 0.177 |
| R-free | 0.20800 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jcq |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.170 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 * | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.078 * | 0.341 * |
| Total number of observations | 278618 * | |
| Number of reflections | 75205 | |
| <I/σ(I)> | 14.4 | 2.1 |
| Completeness [%] | 94.7 * | 82.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 17 * | PEG8K NH4OAc, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | DMSO | 25 (mM) | |
| 3 | 1 | reservoir | ammonium acetate | 200-400 (mM) | |
| 4 | 1 | reservoir | PEG8000 | 12-14 (%) | pH5.3-5.5 |
