5A0U
Structure of CutC choline lyase choline bound form from Klebsiella pneumoniae.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-12-12 |
| Detector | RAYONIX |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 89.410, 221.870, 419.480 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 209.740 - 2.400 |
| R-factor | 0.19083 |
| Rwork | 0.188 |
| R-free | 0.24699 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1r9d |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.565 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 209.740 | 2.460 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.170 | 0.512 |
| Number of reflections | 289262 | |
| <I/σ(I)> | 4.7 | 1.8 |
| Completeness [%] | 93.6 | 87.8 |
| Redundancy | 3 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 20% PEG 3350, 60-20 MM K/NA TARTRATE, 100 MM BIS-TRIS PH 8.5 |
