3R5Z
Structure of a Deazaflavin-dependent reductase from Nocardia farcinica, with co-factor F420
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-28 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.976 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.704, 56.939, 66.003 |
Unit cell angles | 90.00, 105.52, 90.00 |
Refinement procedure
Resolution | 37.515 - 1.503 |
R-factor | 0.1675 |
Rwork | 0.166 |
R-free | 0.19200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3r5y |
RMSD bond length | 0.013 |
RMSD bond angle | 1.490 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER (2.1.4) |
Refinement software | PHENIX (1.5_2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.550 |
High resolution limit [Å] | 1.500 | 3.230 | 1.500 |
Rmerge | 0.080 | 0.036 | 0.473 |
Number of reflections | 42118 | ||
<I/σ(I)> | 18 | 37.803 | 1.559 |
Completeness [%] | 93.5 | 92.6 | 82.1 |
Redundancy | 2.3 | 2.3 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 277 | 30% PEG 2000, 0.1M acetate, 0.2M (NH4)2SO4 with equimolar protein and co-factor, pH 4.6, vapor diffusion, sitting drop, temperature 277K |