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 |
