9BZB
Crystal structure of metallo-hydrolase-like_MBL-fold protein from Salmonella typhimurium LT2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-10-28 |
Detector | DECTRIS PILATUS3 X 6M |
Wavelength(s) | 0.97918 |
Spacegroup name | P 62 |
Unit cell lengths | 120.831, 120.831, 35.339 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.550 - 1.950 |
R-factor | 0.1987 |
Rwork | 0.197 |
R-free | 0.23570 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.569 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.980 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.138 | 0.837 |
Rmeas | 0.147 | 0.990 |
Rpim | 0.048 | 0.518 |
Number of reflections | 21268 | 803 |
<I/σ(I)> | 20.4 | 0.92 |
Completeness [%] | 97.7 | 75.4 |
Redundancy | 7.7 | 2.6 |
CC(1/2) | 0.616 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | 50 mM Tris pH 7.6. 2.9 % (v/v) PEG350 MME, 34.3 % (v/v) PEG 600 |