1O5M
Structure of FPT bound to the inhibitor SCH66336
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-04-02 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 61 |
Unit cell lengths | 171.110, 171.110, 69.310 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.300 |
R-factor | 0.174 |
Rwork | 0.174 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.055 | 0.211 * |
Number of reflections | 49482 | |
<I/σ(I)> | 23.3 | |
Completeness [%] | 95.9 | 71.9 |
Redundancy | 3.5 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 * | 4 * | Wu, Z., (1999) Protein Eng., 12, 341. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | ethanol | 23.6 (mM) | |
2 | 1 | drop | DMSO | 50 (mM) | |
3 | 1 | reservoir | 0.1 (M) | ||
4 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.0 |