3NFB
Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with hydrolyzed ampicillin
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 | 2009-09-16 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 88.300, 97.100, 102.200 |
| Unit cell angles | 90.00, 108.70, 90.00 |
Refinement procedure
| Resolution | 49.300 - 1.850 |
| R-factor | 0.1506 |
| Rwork | 0.150 |
| R-free | 0.17840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n2w |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.050 |
| 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] | 49.300 | 1.900 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.110 | 0.447 |
| Number of reflections | 137090 | |
| <I/σ(I)> | 13 | 3.98 |
| Completeness [%] | 98.4 | 99.1 |
| Redundancy | 3.78 | 3.76 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | 15mg/ml, 1.5M ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
