5VYS
Crystal structure of the WbkC N-formyltransferase (C47S variant) from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-08-25 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 65.927, 65.927, 234.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.965 - 2.200 |
R-factor | 0.18874 |
Rwork | 0.185 |
R-free | 0.25784 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5vyr |
RMSD bond length | 0.013 |
RMSD bond angle | 1.592 |
Data reduction software | SAINT |
Data scaling software | SADABS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.096 | 0.405 |
Number of reflections | 27237 | 3263 |
<I/σ(I)> | 12.3 | 4 |
Completeness [%] | 99.6 | 98.4 |
Redundancy | 14.1 | 8.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 19-25%PEG-5000, 5 mM GDP-perosamine, 5 mM folinic acid, 100 mM MOPS |