1A1A
C-SRC (SH2 DOMAIN WITH C188A MUTATION) COMPLEXED WITH ACE-FORMYL PHOSPHOTYR-GLU-(N,N-DIPENTYL AMINE)
Experimental procedure
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 1994-09 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.400, 65.400, 74.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.000 |
R-factor | 0.198 |
Rwork | 0.198 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1shd |
RMSD bond length | 0.017 |
RMSD bond angle | 23.060 * |
Data reduction software | R-AXIS |
Data scaling software | R-AXIS |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.250 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.064 | 0.132 |
Number of reflections | 18250 | |
<I/σ(I)> | 21.68 | 5.5 |
Completeness [%] | 94.8 | 90 |
Redundancy | 2.7 | 2.99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 1.0 M LI2SO4, 2% PEG8000 AT 4C. THE CRYSTAL WAS SOAKED IN 25% GLYCEROL PRIOR TO DATA COLLECTION., pH 8.0, temperature 277K |
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 | 1.0 (M) | ||
7 | 1 | reservoir | PEG8000 | 2 (%) |