3WT4
Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 4A |
Synchrotron site | PAL/PLS |
Beamline | 4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-04-30 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.99999999 |
Spacegroup name | H 3 |
Unit cell lengths | 134.187, 134.187, 328.756 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 27.400 - 2.300 |
R-factor | 0.14854 |
Rwork | 0.146 |
R-free | 0.19632 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.018 |
RMSD bond angle | 1.917 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.103 | 0.103 |
Number of reflections | 93254 | |
<I/σ(I)> | 11.08 | |
Completeness [%] | 94.9 | 99 |
Redundancy | 3.4 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8 | 295 | 30% PEG400, 0.1M Tris pH 8.0, 0.2M MgCl2, 0.1mM ZnCl2, VAPOR DIFFUSION, temperature 295K |