1PY5
Crystal Structure of TGF-beta receptor I kinase with inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2000-06-10 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.829, 78.111, 90.686 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.258 |
Rwork | 0.258 |
R-free | 0.29200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1b6c |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.440 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.090 | 0.185 |
Number of reflections | 13178 | |
<I/σ(I)> | 8 | 5 |
Completeness [%] | 99.7 | 74.7 |
Redundancy | 6 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.6 | 298 | Tris, ATP, MgCl2, DTT, Hexanediol, PEG4000, LiSO4, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |