5BMO
LnmX protein, a putative GlcNAc-PI de-N-acetylase from Streptomyces atroolivaceus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-04 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9792 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 71.998, 71.998, 284.458 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.000 - 1.920 |
R-factor | 0.1701 |
Rwork | 0.168 |
R-free | 0.21530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3wl4 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.494 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.950 |
High resolution limit [Å] | 1.920 | 5.210 | 1.920 |
Rmerge | 0.084 | 0.049 | 0.699 |
Rmeas | 0.089 | 0.053 | 0.788 |
Rpim | 0.029 | 0.018 | 0.355 |
Total number of observations | 527243 | ||
Number of reflections | 58503 | ||
<I/σ(I)> | 9.3 | 1.99 | |
Completeness [%] | 100.0 | 99.8 | 99.8 |
Redundancy | 9 | 8.8 | 4.7 |
CC(1/2) | 0.998 | 0.713 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 289 | 0.1 M sodium acetate, 0.8 M sodium phosphate, 1.2 di-potassium phosphate |