3NGF
Crystal structure of AP endonuclease, family 2 from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-05-11 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.980, 120.640, 54.680 |
Unit cell angles | 90.00, 117.14, 90.00 |
Refinement procedure
Resolution | 50.010 - 1.800 |
R-factor | 0.143 |
Rwork | 0.141 |
R-free | 0.17600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k77 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.315 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.910 | 1.850 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.045 | |
Number of reflections | 55966 | |
<I/σ(I)> | 14.46 | 3.6 |
Completeness [%] | 98.8 | 93.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 0.04 M KH2PO4, 16% PEG 8000, 20% GLYCEROL, 27 MG/ML PROTEIN, JCSG+ SCREEN WELL D12, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K |