4OIW
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 | SPRING-8 BEAMLINE BL45PX |
Synchrotron site | SPring-8 |
Beamline | BL45PX |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-02-24 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.7321 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 150.020, 218.267, 172.693 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.790 - 2.440 |
R-factor | 0.15044 |
Rwork | 0.148 |
R-free | 0.19650 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4njr |
RMSD bond length | 0.015 |
RMSD bond angle | 1.743 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.440 | 2.550 |
Number of reflections | 95594 | |
Completeness [%] | 99.1 | 99.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | microbatch Crystallization | 7.5 | 295 | 30%(v/v) 2-Propanol, 0.1M Hepes 7.5, 0.2M MgCl2, 10mM Spermidine, 0.1mM ZnCl2, microbatch Crystallization, temperature 295K |