2YQ9
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation V321A, crystallized with 2'-AMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-02-02 |
| Detector | MARRESEARCH MX-165 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.550, 46.790, 107.360 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.426 - 1.900 |
| R-factor | 0.189 |
| Rwork | 0.186 |
| R-free | 0.23580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xmi |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.219 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.070 | 0.670 |
| Number of reflections | 16784 | |
| <I/σ(I)> | 15.3 | 2.5 |
| Completeness [%] | 97.9 | 93.6 |
| Redundancy | 4.9 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4 | 277 | 250 UM PROTEIN AND 10 MM 23-CYCLIC AMP WERE MIXED IN 0.5 PLUS 0.5 DROPS WITH 50 MM SODIUM ACETATE (1:2 PH3:PH5) AND 25% PEG 4000 IN 4C TEMP |
