3NK6
Structure of the Nosiheptide-resistance methyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-06 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.0055 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.884, 69.203, 64.797 |
Unit cell angles | 90.00, 117.85, 90.00 |
Refinement procedure
Resolution | 33.469 - 2.000 |
R-factor | 0.2039 |
Rwork | 0.201 |
R-free | 0.25370 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.216 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.228 | |
Number of reflections | 33406 | |
<I/σ(I)> | 8 | |
Completeness [%] | 97.4 | 95.2 |
Redundancy | 7.1 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 293 | 0.35M ammonium chloride, 24%(w/v) PEG 3350, 0.1M MES, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |