3B3C
Crystal structure of the M180A mutant of the aminopeptidase from Vibrio proteolyticus in complex with leucine phosphonic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Wavelength(s) | 0.90010 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 108.189, 108.189, 97.206 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.630 - 1.460 |
R-factor | 0.198 |
Rwork | 0.197 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3b35 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.203 |
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] | 30.630 |
High resolution limit [Å] | 1.460 |
Number of reflections | 57867 |
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 |