7VEQ
Crystal structure of bacterial chemotaxis-dependent pectin-binding protein SPH1118 in an open conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-10-24 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 1 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 50.855, 151.663, 179.520 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.217 - 1.696 |
Rwork | 0.168 |
R-free | 0.19500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7vev |
RMSD bond length | 0.014 |
RMSD bond angle | 1.707 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | REFMAC |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.217 | 1.740 |
High resolution limit [Å] | 1.696 | 1.700 |
Rmerge | 0.086 | 0.555 |
Number of reflections | 76813 | 10681 |
<I/σ(I)> | 11.1 | 1.87 |
Completeness [%] | 97.8 | |
Redundancy | 5.02 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 2.0 M Ammonium dihydrogenphosphate 0.1 M Tris-HCl 2.0 mM Unsaturated trigalacturonic acid |