3LZN
Crystal Structure Analysis of the apo P19 protein from Campylobacter jejuni at 1.59 A at pH 9
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-21 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 1.282 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 54.396, 73.037, 74.817 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.380 - 1.590 |
| R-factor | 0.14366 |
| Rwork | 0.142 |
| R-free | 0.18413 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | P6222 INCOMPLETE SEMAD MODEL AT 2.8 ANGS RESOLUTION. |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.472 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.110 | 1.680 |
| High resolution limit [Å] | 1.590 | 1.590 |
| Rmerge | 0.037 | 0.655 |
| Number of reflections | 40227 | |
| <I/σ(I)> | 16.6 | 2.2 |
| Completeness [%] | 98.9 | 98.6 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 298 | PROTEIN TREATED WITH 30X EXCESS OF EDTA; WASHED, PRECIPITANT WAS 25-45% POLYETHYLENE GLYCOL (PEG) 350, 0.1 M CHES (2-(N-CYCLOHEXYLAMINO) ETHANE SULFONIC ACID) BUFFER PH 9.0, CRYO FROZEN WITHOUT ANY ADDITION, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K |






