1JCS
CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-05-17 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 |
Unit cell lengths | 170.921, 170.921, 69.425 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.200 |
R-factor | 0.16 |
Rwork | 0.160 |
R-free | 0.20200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1d8d |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.088 * | 0.470 * |
Total number of observations | 207941 * | |
Number of reflections | 58693 * | |
<I/σ(I)> | 17.2 | 2.64 |
Completeness [%] | 99.7 * | 100 |
Redundancy | 5.1 | 4.98 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 17 * | PEG 8000, Ammonium Acetate, DTT, Tris-HCl, pH 5.7, VAPOR DIFFUSION, HANGING DROP at 290K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 14 (%(w/v)) | |
2 | 1 | reservoir | ammonium acetate | 200-600 (mM) | |
3 | 1 | reservoir | dithiothreitol | 20 (mM) |