2CBI
Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 157 |
Detector technology | CCD |
Collection date | 2005-10-31 |
Detector | MARRESEARCH |
Spacegroup name | I 21 21 21 |
Unit cell lengths | 119.939, 147.380, 157.687 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.250 |
R-factor | 0.169 |
Rwork | 0.169 |
R-free | 0.22000 |
Structure solution method | SAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.470 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.330 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.110 | 0.480 |
Number of reflections | 65956 | |
<I/σ(I)> | 7.7 | 7.6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 25.4 | 18.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM CACODYLATE PH 6.5, 30 % PEG 8000) AND 0.25 MICROLITER OF 40 % V/V GAMMA-BUTYROLACTONE TO A 1 PLUS MICROLITER DROP |