3B3V
Crystal structure of the S228A mutant of the aminopeptidase from Vibrio proteolyticus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Wavelength(s) | 0.90010 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 109.317, 109.317, 91.003 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 21.720 - 1.220 |
| R-factor | 0.15 |
| Rwork | 0.149 |
| R-free | 0.17100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1amp |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.670 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 21.720 |
| High resolution limit [Å] | 1.220 |
| Number of reflections | 92234 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | HEPES, KSCN, NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
