2FNU
PseC aminotransferase with external aldimine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-03-28 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 87.600, 145.700, 66.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.500 |
R-factor | 0.15379 |
Rwork | 0.153 |
R-free | 0.17595 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.277 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.500 |
Number of reflections | 122065 |
<I/σ(I)> | 25.3 |
Completeness [%] | 89.9 |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1.5 microL of PseC-product with 1.5 microL of reservoir solution (0.1 M Hepes pH 7.5, 25% PEG 3350), VAPOR DIFFUSION, HANGING DROP, temperature 293K |