5TR7
Crystal structure of a putative D-alanyl-D-alanine carboxypeptidase from Vibrio cholerae O1 biovar eltor str. N16961
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-05 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 31 |
Unit cell lengths | 88.749, 88.749, 85.425 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.050 |
R-factor | 0.19321 |
Rwork | 0.191 |
R-free | 0.23774 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nzo |
RMSD bond length | 0.018 |
RMSD bond angle | 2.028 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | BALBES |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.090 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.066 | 0.750 |
Number of reflections | 47191 | |
<I/σ(I)> | 36.6 | 3.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.8 | 5.7 |
CC(1/2) | 0.970 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 0.2 M Sodium Nitrate, 0.1 M Bis-Tris propane, 20% PEG3350 |