7CRM
Aminoglycoside 2'-N-acetyltransferase from Mycolicibacterium smegmatis-APO Structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 5C (4A) |
Synchrotron site | PAL/PLS |
Beamline | 5C (4A) |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-10-31 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9794 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 69.008, 81.212, 129.768 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.421 - 2.487 |
R-factor | 0.1968 |
Rwork | 0.193 |
R-free | 0.26940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m44 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.948 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.540 |
High resolution limit [Å] | 2.487 | 2.500 |
Rmerge | 0.113 | 0.475 |
Number of reflections | 26178 | 1297 |
<I/σ(I)> | 31.7 | |
Completeness [%] | 99.8 | 100 |
Redundancy | 6.6 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.2M ammonium acetate, 0.1M Bis-Tris (pH 6.5), 20% (w/v) PEG 3350 |