1LD8
Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 49
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-02-29 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 |
Unit cell lengths | 178.134, 178.134, 64.461 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 * - 1.800 |
R-factor | 0.184 * |
Rwork | 0.184 |
R-free | 0.20200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jcq |
RMSD bond length | 0.005 * |
RMSD bond angle | 1.176 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 * | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.059 * | 0.170 * |
Total number of observations | 242857 * | |
Number of reflections | 87139 * | |
Completeness [%] | 80.5 * | 16 * |
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 | reservoir | ammonium acetate | 200-400 (mM) | |
2 | 1 | reservoir | PEG8000 | 12-14 (%) | pH5.3-5.5 |
3 | 1 | drop | protein | 10 (mg/ml) |