6F2P
Structure of Paenibacillus xanthan lyase to 2.6 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-08-11 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.0000 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 100.610, 100.610, 324.830 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.053 - 2.600 |
R-factor | 0.167 |
Rwork | 0.165 |
R-free | 0.21290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2e24 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.990 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.053 | 2.670 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmeas | 0.208 | 1.388 |
Number of reflections | 51793 | 3728 |
<I/σ(I)> | 11.43 | 1.82 |
Completeness [%] | 98.5 | 97.9 |
Redundancy | 8.1 | 7.3 |
CC(1/2) | 0.994 | 0.687 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 277 | Protein: 4 mg/mL. Reservoir: 0.2 M CaCl2, 0.1 M Bis-Tris pH5.5, 45 %v/v MPD. 100 uL Drop: 75 % protein 25 % reservour. 0.3 uL |