5LP4
Penicillin-Binding Protein (PBP2) from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 273 |
| Detector technology | CCD |
| Collection date | 2013-07-04 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979526 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.397, 140.965, 81.297 |
| Unit cell angles | 90.00, 101.67, 90.00 |
Refinement procedure
| Resolution | 45.390 - 3.030 |
| R-factor | 0.25467 |
| Rwork | 0.251 |
| R-free | 0.28766 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pbn |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.268 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.390 | 3.210 |
| High resolution limit [Å] | 3.030 | 3.030 |
| Rmerge | 0.430 | |
| Number of reflections | 27837 | |
| <I/σ(I)> | 12.15 | 3.01 |
| Completeness [%] | 90.8 | 84.5 |
| Redundancy | 3 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 1.4M (NH4)2SO4, 50MM HEPES-NA PH 7 |
