2SRC
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC, IN COMPLEX WITH AMP-PNP
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.590, 72.970, 172.690 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 * |
R-factor | 0.226 |
Rwork | 0.226 |
R-free | 0.28100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fmk |
RMSD bond length | 0.007 |
RMSD bond angle | 1.270 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 1.800 |
Rmerge | 0.051 * |
Total number of observations | 296913 * |
Number of reflections | 55186 |
Completeness [%] | 93.2 |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | pH 6.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
10 | 1 | reservoir | dithiothreitol | 10 (mM) | |
11 | 1 | reservoir | PEG4000 | 8 (%) | |
2 | 1 | drop | HEPES | 20 (mM) | |
3 | 1 | drop | 0.1 (M) | ||
4 | 1 | drop | dithiothreitol | 5 (mM) | |
5 | 1 | drop | AMP-PNP | 0.1 (M) | |
6 | 1 | drop | peptide | 22 (mM) | |
7 | 1 | drop | Tris-HCl | 0.1 (M) | |
8 | 1 | reservoir | MES | 50 (mM) | |
9 | 1 | reservoir | 10 (mM) |