7EFT
Crystal structure of cell shape-determining protein MreC
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 | 2019-01-10 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9785 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 133.291, 47.583, 77.332 |
Unit cell angles | 90.00, 99.18, 90.00 |
Refinement procedure
Resolution | 29.851 - 2.100 |
R-factor | 0.19 |
Rwork | 0.186 |
R-free | 0.23590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2j5u |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.140 |
High resolution limit [Å] | 2.100 | 5.690 | 2.100 |
Rmerge | 0.104 | 0.042 | 0.474 |
Rmeas | 0.127 | 0.050 | 0.591 |
Rpim | 0.071 | 0.028 | 0.347 |
Total number of observations | 83716 | ||
Number of reflections | 27893 | 1478 | 1309 |
<I/σ(I)> | 3.2 | ||
Completeness [%] | 98.9 | 99.4 | 94 |
Redundancy | 3 | 3.1 | 2.6 |
CC(1/2) | 0.998 | 0.699 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 291 | 9.9% Isopropanol, 9.9% (v/v) PEG3350, 0.1M Tris-HCl pH 8.5 |