2XHN
Rhamnogalacturonan lyase from Aspergillus aculeatus K150A active site mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-5 |
Synchrotron site | MAX II |
Beamline | I911-5 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-02-16 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 108.934, 108.978, 170.650 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.007 - 1.520 |
R-factor | 0.1159 |
Rwork | 0.113 |
R-free | 0.16440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nkg |
RMSD bond length | 0.009 |
RMSD bond angle | 1.240 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHENIX (AUTOMR) |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.570 |
High resolution limit [Å] | 1.520 | 1.520 |
Rmerge | 0.060 | 0.150 |
Number of reflections | 142062 | |
<I/σ(I)> | 24 | 9.7 |
Completeness [%] | 91.6 | 86 |
Redundancy | 4.9 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 20% PEG 4000, 0.1 AMMONIUM SULFATE, HANGING DROP VAPOR DIFFUSION |