3BRB
Crystal structure of catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with ADP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-07-06 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.91790 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.385, 89.880, 69.537 |
Unit cell angles | 90.00, 103.09, 90.00 |
Refinement procedure
Resolution | 25.050 - 1.900 |
R-factor | 0.19469 |
Rwork | 0.192 |
R-free | 0.24000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2p0c |
RMSD bond length | 0.013 |
RMSD bond angle | 1.511 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.050 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 49802 | |
<I/σ(I)> | 24.1 | 2.3929 |
Completeness [%] | 98.3 | 88.7 |
Redundancy | 7.2 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 290 | MER protein (38 mg/mL) was pre-incubated with 2.5 mM ATP and 10 mM MgCl2 for 3 hours at room temperature. Crystals were obtained at 290K against 29% PEG 400, 0.2M MgCl2, and 0.1 M Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP |