3N2W
Crystal structure of the N-terminal beta-aminopeptidase BapA from Sphingosinicella xenopeptidilytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2008-01-28 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0060 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 87.360, 96.720, 101.420 |
| Unit cell angles | 90.00, 108.23, 90.00 |
Refinement procedure
| Resolution | 48.809 - 1.450 |
| R-factor | 0.1314 |
| Rwork | 0.131 |
| R-free | 0.14980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1b65 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.438 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.809 | 1.470 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.075 | 0.575 |
| Number of reflections | 278550 | |
| <I/σ(I)> | 16.99 | 2.67 |
| Completeness [%] | 98.5 | 92.3 |
| Redundancy | 3.2 | 2.32 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | 1.5M Ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
