2CBJ
Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase in complex with PUGNAc
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 157 |
Detector technology | IMAGE PLATE |
Collection date | 2005-11-09 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | I 21 21 21 |
Unit cell lengths | 129.613, 145.745, 152.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.350 |
R-factor | 0.194 |
Rwork | 0.193 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cbi |
RMSD bond length | 0.013 |
RMSD bond angle | 1.366 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.430 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.080 | 0.610 |
Number of reflections | 56462 | |
<I/σ(I)> | 15.8 | 2.6 |
Completeness [%] | 93.7 | 96 |
Redundancy | 3.9 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM CACODYLATE PH 6.5 AND 30 % PEG 8000) AND 0.25 MICROLITERS OF 40 % V/V GAMMA-BUTYROLACTONE ADDED TO A 1 PLUS 1 MICROLITER DROP |