5K3W
Structural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-09-06 |
Detector | DECTRIS PILATUS 2M |
Wavelength(s) | 0.9717 |
Spacegroup name | P 62 |
Unit cell lengths | 154.428, 154.428, 71.005 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 48.680 - 2.503 |
R-factor | 0.1655 |
Rwork | 0.163 |
R-free | 0.21810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3sno |
RMSD bond length | 0.007 |
RMSD bond angle | 0.819 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.700 | 2.650 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.211 | 0.604 |
Number of reflections | 31759 | |
<I/σ(I)> | 5.5 | 2.1 |
Completeness [%] | 94.8 | 96.3 |
Redundancy | 3.9 | 3.8 |
CC(1/2) | 0.971 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 2.4 M sodium malonate pH 7.0 microseeding |