1QBQ
STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 1997-10-06 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 61 |
Unit cell lengths | 174.132, 174.132, 69.705 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.400 |
R-factor | 0.218 * |
Rwork | 0.218 |
R-free | 0.29200 |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.061 | 0.371 |
Total number of observations | 144714 * | |
Number of reflections | 42739 | |
<I/σ(I)> | 20 | |
Completeness [%] | 90.0 | 57 |
Redundancy | 3.3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.7 * | 22 * | 7% PEG 4000, 0.1 M sodium acetate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris | 20 (mM) | |
2 | 1 | drop | dithiothreitol | 1 (mM) | |
3 | 1 | drop | 20 (mM) | ||
4 | 1 | drop | 0.010 (mM) | ||
5 | 1 | drop | protain | 25 (mg/ml) | |
6 | 1 | reservoir | PEG4000 | 7 (%) | |
7 | 1 | reservoir | sodium acetate | 0.1 (M) | |
8 | 1 | reservoir | dithiothreitol | 200 (mM) |