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 |