4YFV
X-ray structure of the 4-N-formyltransferase VioF from Providencia alcalifaciens O30
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-05-15 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 2 |
Unit cell lengths | 132.962, 132.962, 159.411 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.720 - 1.890 |
R-factor | 0.18362 |
Rwork | 0.181 |
R-free | 0.23753 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4nv1 |
RMSD bond length | 0.011 |
RMSD bond angle | 2.077 |
Data reduction software | SAINT |
Data scaling software | SADABS |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.940 |
High resolution limit [Å] | 1.890 | 1.890 |
Rmerge | 0.067 | 0.379 |
Number of reflections | 43314 | |
<I/σ(I)> | 17 | 3.4 |
Completeness [%] | 99.8 | 6.9 |
Redundancy | 6.8 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 8-10% PEG-8000, 1 M tetramethylammonium chloride, 100 mM Hepes |