3VH9
Crystal structure of Aeromonas proteolytica aminopeptidase complexed with 8-quinolinol
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-30 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 108.463, 108.463, 90.737 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 13.618 - 1.290 |
| R-factor | 0.1324 |
| Rwork | 0.131 |
| R-free | 0.15340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PEB ENTRY 1LOK |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.451 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.310 |
| High resolution limit [Å] | 1.290 | 1.290 |
| Rmerge | 0.068 | 0.358 |
| Number of reflections | 79004 | |
| <I/σ(I)> | 65.9 | 8.6 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 21.4 | 21 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 100mM Tris-HCl, 100mM KSCN, 4.5M NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
