4E3Q
PMP-bound form of Aminotransferase crystal structure from Vibrio fluvialis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-09-01 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 63.071, 162.182, 180.398 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.790 - 1.900 |
R-factor | 0.1759 |
Rwork | 0.174 |
R-free | 0.20980 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.040 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | BUSTER (2.9.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.000 | 1.900 |
Number of reflections | 144629 | |
Completeness [%] | 98.9 | 98.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | 20% PEG8000, 0.2M Lithium Sulfate, 0.1M bis-tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |