3ERK
THE COMPLEX STRUCTURE OF THE MAP KINASE ERK2/SB220025
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01 |
Detector | RIGAKU |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.850, 70.000, 60.700 |
Unit cell angles | 90.00, 109.20, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ERK |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.100 | 2.000 |
Rmerge | 0.028 * | 0.282 * |
Number of reflections | 22843 | |
<I/σ(I)> | 20 | 3 |
Completeness [%] | 88.0 | 90 |
Redundancy | 2.5 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.4 * | Wang, Z., (1997) Proc. Natl. Acad. Sci. USA, 94, 2327. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
10 | 1 | reservoir | 0.2 (M) | ||
11 | 1 | reservoir | HEPES | 0.1 (M) | |
2 | 1 | drop | 50 (mM) | ||
3 | 1 | drop | EDTA | 1 (mM) | |
4 | 1 | drop | dithiothreitol | 10 (mM) | |
5 | 1 | drop | benzamidine | 1 (mM) | |
6 | 1 | drop | pepstasin | 0.001 (mM) | |
7 | 1 | drop | leupeptin | 0.01 (mM) | |
8 | 1 | drop | HEPES | 25 (mM) | |
9 | 1 | reservoir | PEG8000 | 18 (%) |