5G2P
The crystal structure of a S-selective transaminase from Arthrobacter sp.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-06-06 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.398, 142.662, 99.681 |
Unit cell angles | 90.00, 105.33, 90.00 |
Refinement procedure
Resolution | 46.840 - 1.890 |
R-factor | 0.15882 |
Rwork | 0.157 |
R-free | 0.20048 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gju |
RMSD bond length | 0.011 |
RMSD bond angle | 1.403 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.100 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.090 | 0.640 |
Number of reflections | 137172 | |
<I/σ(I)> | 14.1 | 2.2 |
Completeness [%] | 99.8 | 92.4 |
Redundancy | 4.2 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | 15% PEG3350 0.2 M NA-MALONATE 100 MM MMT BUFFER (DL-MALIC ACID, MES AND TRIS BASE) PH 5.0) 10 MM PLP |