2A2A
High-resolution crystallographic analysis of the autoinhibited conformation of a human death-associated protein kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-10 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9206 |
Spacegroup name | P 1 |
Unit cell lengths | 55.300, 60.650, 98.710 |
Unit cell angles | 92.16, 103.45, 94.25 |
Refinement procedure
Resolution | 20.000 - 1.470 |
R-factor | 0.15016 |
Rwork | 0.150 |
R-free | 0.20688 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2a27 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.599 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.520 |
High resolution limit [Å] | 1.470 | 1.470 |
Number of reflections | 200389 | |
<I/σ(I)> | 11.1 | 1.9 |
Completeness [%] | 94.8 | 93.4 |
Redundancy | 2.5 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | PEG4000, glycerol, DTT, Tris, lithium sulfate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |