6DXP
The crystal structure of an FMN-dependent NADH-azoreductase from Klebsiella pneumoniae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-02-07 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97931 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 133.668, 97.323, 77.534 |
Unit cell angles | 90.00, 90.71, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.478 |
R-factor | 0.2396 |
Rwork | 0.237 |
R-free | 0.28490 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1v4b |
RMSD bond length | 0.010 |
RMSD bond angle | 1.589 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (0.5.32) |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.170 | 29.170 | 2.610 |
High resolution limit [Å] | 2.478 | 7.840 | 2.480 |
Rmerge | 0.100 | 0.029 | 0.642 |
Rmeas | 0.117 | 0.034 | 0.777 |
Rpim | 0.060 | 0.018 | 0.432 |
Number of reflections | 34876 | 1136 | 4695 |
<I/σ(I)> | 5.6 | ||
Completeness [%] | 98.6 | 97.2 | 91.5 |
Redundancy | 3.7 | 3.6 | 3.1 |
CC(1/2) | 0.996 | 0.998 | 0.736 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6 | 291 | 0.1M MES pH 6.0, 25% PEG 8000, 0.2M calcium acetate |