6HC6
The structure of BSAP, a zinc aminopeptidase from Bacillus subtilis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-12-15 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.954 |
| Spacegroup name | P 63 |
| Unit cell lengths | 224.922, 224.922, 42.502 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.697 - 1.770 |
| R-factor | 0.1656 |
| Rwork | 0.165 |
| R-free | 0.20270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cp7 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.823 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.700 | 1.800 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.068 | 0.109 |
| Number of reflections | 120817 | |
| <I/σ(I)> | 18.9 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 9.3 | 8.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 20% PEG 2K MME, 0.1M LiSO4, 4mM MnCl2, 0.1M acetate pH 5.6 |
