2H6H
Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A
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 | 2005-02-28 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.067401 |
Spacegroup name | P 61 |
Unit cell lengths | 178.782, 178.782, 64.587 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.590 - 1.800 |
R-factor | 0.177 |
Rwork | 0.177 |
R-free | 0.18000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jcq |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 109005 | |
<I/σ(I)> | 25.5 | 6.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 9.2 | 9.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 290 | 14% PEG 8000, 200 mM ammonium acetate pH 5.2, 20 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 290K |