1HMU
ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-02-02 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 86.900, 86.900, 192.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
Rwork | 0.227 |
R-free | 0.26600 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.340 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.063 | 0.302 |
Total number of observations | 282695 * | |
Number of reflections | 49755 | |
<I/σ(I)> | 14.3 | |
Completeness [%] | 98.6 | 98.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | PEG 3350, sodium acetate, hepes , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG3350 | 15 (%(w/v)) | |
2 | 1 | reservoir | sodium acetate | 400 (mM) | |
3 | 1 | reservoir | HEPES | 100 (mM) |