3LZO
Crystal Structure Analysis of the copper-reconstituted P19 protein from Campylobacter jejuni at 1.65 A at pH 10.0
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 55.831, 72.581, 78.817 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.340 - 1.650 |
| R-factor | 0.14118 |
| Rwork | 0.139 |
| R-free | 0.18685 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | P6222 incomplete SeMAD model at 2.8 A resolution. |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.523 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.340 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.040 | 0.661 |
| Number of reflections | 39217 | |
| <I/σ(I)> | 20.2 | 2.4 |
| Completeness [%] | 99.5 | 98.7 |
| Redundancy | 4.7 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 10 | 298 | 25-45% POLYETHYLENE GLYCOL (PEG) 350, 0.1 M CHES (2-(N-CYCLOHEXYLAMINO) ETHANE SULFONIC ACID) BUFFER PH 10.0, CRYO FROZEN WITHOUT ANY ADDITION, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K |






