1KZO
PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-03-07 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 61 |
| Unit cell lengths | 171.199, 171.199, 69.444 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.200 |
| R-factor | 0.159 |
| Rwork | 0.159 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1d8d |
| RMSD bond length | 0.007 |
| RMSD bond angle | 20.900 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.851) |
| 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 | 0.089 * | 0.560 * |
| Total number of observations | 253335 * | |
| Number of reflections | 56209 | |
| <I/σ(I)> | 16.1 | 1.8 |
| Completeness [%] | 96.0 | 87.9 |
| Redundancy | 4.51 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 17 * | Long, S.B., (2000) Structure, 8, 209. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 12-16 (%(w/v)) | |
| 2 | 1 | reservoir | ammonium acetate | 600 (mM) | |
| 3 | 1 | reservoir | dithiothreitol | 20 (mM) |
