1BL6
THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB216995
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01-07 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.570, 84.710, 123.540 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.25100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MAP KINASE P38 |
RMSD bond length | 0.008 |
RMSD bond angle | 25.540 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE ((CCP4)) |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.200 | 2.540 |
High resolution limit [Å] | 2.450 | 2.450 |
Rmerge | 0.054 * | 0.324 |
Total number of observations | 344423 * | |
Number of reflections | 18307 | |
<I/σ(I)> | 21 | 3.6 |
Completeness [%] | 98.2 | 90.1 |
Redundancy | 18.8 |
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 (%) |