7CXS
Crystal structure of CmnK, a L-Dap formation enzyme in capreomycin biosynthesis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2020-07-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9732 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 50.106, 87.080, 146.137 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.973 - 1.830 |
R-factor | 0.1874 |
Rwork | 0.186 |
R-free | 0.22020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4mp3 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.421 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.900 |
High resolution limit [Å] | 1.830 | 1.830 |
Number of reflections | 56430 | 5363 |
<I/σ(I)> | 42.6 | |
Completeness [%] | 98.6 | |
Redundancy | 5.9 | |
CC(1/2) | 0.990 | 0.970 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 50 mM MgCl2.6H2O, 30% w/v PEG-550, and 100 mM HEPES |