3DFC
Crystal structure of a glycine-rich loop mutant of the death associated protein kinase catalytic domain with AMPPNP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.688, 62.444, 88.602 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.16793 |
| Rwork | 0.165 |
| R-free | 0.23048 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jks |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.546 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.080 | 0.605 |
| Number of reflections | 21129 | |
| <I/σ(I)> | 3.2 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.2 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.2M lithium nitrate, 2.2 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
