4TT7
Crystal structure of human ALK with a covalent modification
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-12-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9774 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.535, 57.157, 104.216 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.200 - 2.100 |
R-factor | 0.19458 |
Rwork | 0.192 |
R-free | 0.24403 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2xp2 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.197 |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.200 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.135 | 0.621 |
Number of reflections | 18384 | |
<I/σ(I)> | 10.1 | 2.8 |
Completeness [%] | 98.8 | 97.5 |
Redundancy | 5.6 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 2 uL of 17 mg/mL protein (50 mM Bicine pH 8.4, 150 mM NaCl, 5 mM DTT) with 2 uL of 0.1 M TRIS hydrochloride, 0.2 M Sodium acetate trihydrate, 30% w/v Polyethylene glycol 4,000 |