6B8C
Crystal structure of NlpC/p60 domain of peptidoglycan hydrolase SagA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-1 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-1 |
Temperature [K] | 298 |
Detector technology | PIXEL |
Collection date | 2017-03-16 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.97930 |
Spacegroup name | P 4 3 2 |
Unit cell lengths | 100.385, 100.385, 100.385 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.894 - 2.403 |
R-factor | 0.2426 |
Rwork | 0.239 |
R-free | 0.26920 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fdy |
RMSD bond length | 0.003 |
RMSD bond angle | 0.640 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.400 |
Rpim | 0.035 |
Number of reflections | 8107 |
<I/σ(I)> | 38.5 |
Completeness [%] | 100.0 |
Redundancy | 10.2 |
CC(1/2) | 0.997 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 2 M ammonium sulfate, 0.1 M Bis-Tris |