2WLT
The crystal structure of Helicobacter pylori L-asparaginase at 1.4 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X13 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-08-17 |
Detector | MARRESEARCH SX-165 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 63.559, 94.796, 100.342 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.400 |
R-factor | 0.1312 |
R-free | 0.16870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wsa |
RMSD bond length | 0.012 |
RMSD bond angle | 0.032 |
Data reduction software | HKL |
Data scaling software | HKL |
Phasing software | PHASER |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.100 | 0.270 |
Number of reflections | 59013 | |
<I/σ(I)> | 22.8 | 7.2 |
Completeness [%] | 99.7 | 99.1 |
Redundancy | 7.1 | 8.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | PROTEIN WAS CRYSTALLIZED FROM 17.5% W/V PEG 4000, 0.1 M MG FORMATE, 0.1 M HEPES-NAOH, PH 7.0 |