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 |