6OCQ
Crystal structure of RIP1 kinase in complex with a pyrrolidine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-10-03 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.07 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.297, 95.117, 127.240 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 76.183 - 2.793 |
| R-factor | 0.2059 |
| Rwork | 0.203 |
| R-free | 0.26810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.211 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 95.120 | 95.120 | 2.940 |
| High resolution limit [Å] | 2.790 | 8.830 | 2.790 |
| Rmerge | 0.060 | 0.024 | 0.534 |
| Rmeas | 0.068 | 0.028 | 0.598 |
| Rpim | 0.030 | 0.013 | 0.266 |
| Total number of observations | 70273 | 2082 | 10390 |
| Number of reflections | 14805 | 526 | 2113 |
| <I/σ(I)> | 17 | 42.2 | 2.5 |
| Completeness [%] | 99.7 | 96.7 | 100 |
| Redundancy | 4.7 | 4 | 4.9 |
| CC(1/2) | 0.999 | 0.999 | 0.814 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 24 % PEG 4000, 0.1 M ammonium acetate, 0.1 M HEPES pH 7.5 |
