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 |
