1FPP
PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 |
| Unit cell lengths | 170.000, 170.000, 68.860 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 12.000 - 2.750 |
| R-factor | 0.24 |
| Rwork | 0.230 |
| R-free | 0.30000 |
| Structure solution method | MIR |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.000 | 2.850 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Rmerge | 0.049 * | 0.134 * |
| Number of reflections | 24856 | |
| <I/σ(I)> | 15 | 8 |
| Completeness [%] | 84.0 | 85 |
| Redundancy | 1.9 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 4 * | protein solution was mixed with an equal volume of precipitant * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 20 (mg/ml) | |
| 2 | 1 | drop | compound | 1 (mM) | |
| 3 | 1 | drop | Tris-HCl | 20 (mM) | |
| 4 | 1 | drop | 10 (mM) | ||
| 5 | 1 | drop | 0.02 (mM) | ||
| 6 | 1 | drop | dithiothreitol | 10 (mM) | |
| 7 | 1 | reservoir | 0.4 (M) | precipitant | |
| 8 | 1 | reservoir | dithiothreitol | 10 (mM) | precipitant |
