1A1C
C-SRC (SH2 DOMAIN) COMPLEXED WITH ACE-PHOSPHOTYR-GLU-(N-ME(-(CH2)3-CYCLOPENTYL))
Experimental procedure
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 1994-03 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.700, 66.900, 75.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.400 |
R-factor | 0.186 |
Rwork | 0.186 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1shd |
RMSD bond length | 0.017 |
RMSD bond angle | 23.241 * |
Data reduction software | bioteX |
Data scaling software | bioteX |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.061 | 0.178 |
Number of reflections | 9865 | |
<I/σ(I)> | 11 | 3.4 |
Completeness [%] | 91.0 | 83 |
Redundancy | 3.2 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | 22 * | PROTEIN WAS CRYSTALLIZED FROM 0.1 M ACETATE, PH 4.6,2M AMMONIUM SULFATE AT 22 C., temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 125 (mg/ml) | |
2 | 1 | drop | HEPES | 20 (mM) | |
3 | 1 | drop | 350 (mM) | ||
4 | 1 | drop | dithiothreitol | 5 (mM) | |
5 | 1 | drop | EDTA | 5 (mM) | |
6 | 1 | reservoir | acetate | 0.1 (M) | |
7 | 1 | reservoir | ammonium sulfate | 2 (M) |