1LY8
The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-04-27 |
Detector | MARRESEARCH |
Wavelength(s) | 1.08535 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 74.490, 114.860, 73.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.910 - 2.050 |
R-factor | 0.202 |
Rwork | 0.202 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.014 |
RMSD bond angle | 21.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.100 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.086 | 0.186 |
Total number of observations | 110655 * | |
Number of reflections | 35855 | |
Completeness [%] | 91.6 * | 89.4 * |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 5.5 * | 277 | 1.6M ammonium sulphate, 0.1M 2-(N- Morpholino)ethanesulfonic acid, pH 6.2, VAPOR DIFFUSION, HANGING DROP at 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | ammonium sulfate | 1.5 (M) | |
2 | 1 | drop | sodium acetate | 0.1 (M) | pH5.5 |
3 | 1 | reservoir | MES | 0.1 (M) | pH6.2 |
4 | 1 | reservoir | ammonium sulfate | 1.6 (M) |