1FMK
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.759, 87.380, 101.295 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.26400 |
Structure solution method | MULTIPLE ISOMORPHOUS HEAVY-ATOM REPLACEMENT (MIR) METHOD. THREE DERIVATIVES USED FOR PHASING. |
RMSD bond length | 0.010 |
RMSD bond angle | 1.160 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 1.500 |
Rmerge | 0.053 * |
Total number of observations | 102852 * |
Number of reflections | 25752 * |
Completeness [%] | 90.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PIPES | 50 (mM) | |
3 | 1 | reservoir | sodium tartrate | 0.8 (M) | |
4 | 1 | reservoir | dithiothreitol | 20 (mM) |