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 |