2H6F
Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-03-29 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.97920 |
Spacegroup name | P 61 |
Unit cell lengths | 178.572, 178.572, 64.660 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.660 - 1.500 |
R-factor | 0.19 |
Rwork | 0.190 |
R-free | 0.20300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jcq |
RMSD bond length | 0.004 |
RMSD bond angle | 1.160 |
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 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 184708 | |
<I/σ(I)> | 25.2 | 2.5 |
Completeness [%] | 99.0 | 98.2 |
Redundancy | 7.14 | 5.6 |
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 |