4CWM
High-glycosylation crystal structure of the bifunctional endonuclease (AtBFN2) from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-10-10 |
Detector | ADSC QUANTUM |
Spacegroup name | P 1 |
Unit cell lengths | 45.375, 52.706, 61.105 |
Unit cell angles | 71.34, 78.57, 76.74 |
Refinement procedure
Resolution | 23.280 - 2.090 |
R-factor | 0.20108 |
Rwork | 0.197 |
R-free | 0.26802 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3w52 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.564 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.280 | 2.150 |
High resolution limit [Å] | 2.090 | 2.090 |
Rmerge | 0.010 | 0.450 |
Number of reflections | 28226 | |
<I/σ(I)> | 14.7 | 3.7 |
Completeness [%] | 97.3 | 88 |
Redundancy | 3.9 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 0.1 M TRIS PH 8.5 0.2 M SODIUM ACETATE 30% W/V PEG4000 |