3I5Z
Crystal structure of ERK2 bound to (S)-N-(2-hydroxy-1-phenylethyl)-4-(5-methyl-2-(phenylamino)pyrimidin-4-yl)-1H-pyrrole-2-carboxamide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-06-07 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.948, 70.751, 118.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 60.740 - 2.200 |
R-factor | 0.217 |
Rwork | 0.214 |
R-free | 0.25800 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | in-house unpublished structure |
RMSD bond length | 0.009 |
RMSD bond angle | 1.156 |
Data reduction software | DENZO |
Data scaling software | d*TREK |
Phasing software | REFMAC (5.5.0072) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 91.000 | 91.000 | 2.260 |
High resolution limit [Å] | 2.200 | 5.040 | 2.200 |
Rmerge | 0.073 | 0.044 | 0.301 |
Number of reflections | 18555 | ||
<I/σ(I)> | 12.3 | ||
Completeness [%] | 95.2 | 98.8 | 75.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 298 | Protein: 14 mg/ml, 20 mM Tris-HCl pH 7.0, 5 mM DTT, 200 mM NaCl. Precipitant: 100 mM HEPES pH 7.2, 28-30% PEG MME 2000, 200 mM Ammonium sulfate, 20 mM 2-Mercaptoethanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K |