2YPE
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3'- cyclic AMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Collection date | 2012-04-03 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 40.800, 47.130, 53.780 |
| Unit cell angles | 90.00, 94.28, 90.00 |
Refinement procedure
| Resolution | 9.996 - 1.900 |
| R-factor | 0.1687 |
| Rwork | 0.167 |
| R-free | 0.20700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xmi |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.690 |
| 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] | 10.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.100 | 1.010 |
| Number of reflections | 16037 | |
| <I/σ(I)> | 13.5 | 1.5 |
| Completeness [%] | 98.8 | 98.5 |
| Redundancy | 4.2 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4 | 277 | 250 UM PROTEIN AND 10 MM 23-CYCLIC AMP MIXED IN 0.5 PLUS 0.5 DROPS WITH 50 MM SODIUM ACETATE (1:1, PH3:PH5) AND 23% PEG 4000 IN 4C TEMP |






