1SA5
Rat protein farnesyltransferase complexed with FPP and BMS-214662
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-04 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 61 |
Unit cell lengths | 170.469, 170.469, 69.028 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.210 - 2.600 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1d8d |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 35102 | |
<I/σ(I)> | 11.8 | 3.7 |
Completeness [%] | 98.7 | 97.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.7 | 290 | 14% PEG 8000, 400 mM ammonium acetate pH 5.7, 20 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 290K, pH 5.70 |