8DVH
Crystal structure of ATP-dependent Lon protease from Bacillus subtillis (BsLonBA)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-09-17 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 63 |
Unit cell lengths | 89.892, 89.892, 83.950 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 77.850 - 1.900 |
R-factor | 0.1954 |
Rwork | 0.194 |
R-free | 0.23710 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rre |
RMSD bond length | 0.010 |
RMSD bond angle | 1.687 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 84.000 | 1.940 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.044 | |
Number of reflections | 294057 | 1942 |
<I/σ(I)> | 30.1 | |
Completeness [%] | 99.9 | |
Redundancy | 9.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | 35% PEG400 at pH 7.8 |