3B35
Crystal structure of the M180A 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 |
Temperature [K] | 100 |
Wavelength(s) | 0.90010 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 109.148, 109.148, 90.990 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.000 - 1.100 |
R-factor | 0.15 |
Rwork | 0.149 |
R-free | 0.16600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1amp |
RMSD bond length | 0.012 |
RMSD bond angle | 1.533 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.000 | |
High resolution limit [Å] | 1.100 | 1.100 |
Rmerge | 0.059 | |
Number of reflections | 122065 | |
<I/σ(I)> | 2 |
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 |