1K9A
Crystal structure analysis of full-length carboxyl-terminal Src kinase at 2.5 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-06-09 |
Detector | OXFORD PX210 |
Wavelength(s) | 0.900 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 115.000, 162.600, 232.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 73.500 - 2.500 |
R-factor | 0.246 |
Rwork | 0.246 |
R-free | 0.28800 |
Structure solution method | SIRAS |
RMSD bond length | 0.007 |
RMSD bond angle | 1.427 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 73.000 * | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.073 | 0.398 |
Number of reflections | 150489 | 17029 * |
<I/σ(I)> | 6.9 | 1.7 |
Completeness [%] | 98.2 | 98.2 |
Redundancy | 5 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 288 | ammonium sulphate, HEPES buffer, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 288K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | reservoir | HEPES-NaOH | 50 (mM) | pH7.4 |
3 | 1 | reservoir | ammonium sulfate | 1.90-1.95 (M) |