3FFH
The crystal structure of histidinol-phosphate aminotransferase from Listeria innocua Clip11262.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-08-07 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97940 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.456, 83.671, 122.773 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.850 - 2.310 |
R-factor | 0.20838 |
Rwork | 0.206 |
R-free | 0.25211 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.472 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SHELXD |
Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.000 | 2.450 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.180 | 0.651 |
Number of reflections | 34738 | |
<I/σ(I)> | 12.6 | 1.6 |
Completeness [%] | 96.0 | 77.3 |
Redundancy | 5.3 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.2M MgSO4 20% PEG4000 10% Glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 289K |