2F0Y
Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-09-20 |
Detector | MACSCIENCE |
Wavelength(s) | 1.0 |
Spacegroup name | P 61 |
Unit cell lengths | 171.888, 171.888, 71.367 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.700 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.319 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.750 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 29887 | |
Completeness [%] | 98.7 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.3 | 295 | 0.1M Na Aetate, pH 5.1, 0.2M NaCl, 10% isopropyl alcohol , pH 5.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K |