6LM2
Crystal structure of Zinc binding protein ZinT from E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL18U1 |
Synchrotron site | SSRF |
Beamline | BL18U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-11-25 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9793 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 55.810, 55.810, 153.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.355 - 2.130 |
R-factor | 0.228154334809 |
Rwork | 0.226 |
R-free | 0.27471 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5yxc |
RMSD bond length | 0.007 |
RMSD bond angle | 0.863 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.130 | 2.190 |
High resolution limit [Å] | 2.130 | 2.130 |
Number of reflections | 14365 | 1138 |
<I/σ(I)> | 17.4 | |
Completeness [%] | 99.9 | |
Redundancy | 24.6 | |
CC(1/2) | 0.998 | 0.974 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.2 M Zinc acetate, 0.1 M Sodium acetate pH 4.5, 10 %(w/v) PEG 3000 |