4WCN
Crystal Structure of Tripeptide bound Cell Shape Determinant Csd4 protein from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08B1-1 |
| Synchrotron site | CLSI |
| Beamline | 08B1-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-11-21 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.230, 66.830, 145.050 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.146 - 1.750 |
| R-factor | 0.1787 |
| Rwork | 0.177 |
| R-free | 0.20820 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.334 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 49.150 | 1.800 | |
| High resolution limit [Å] | 1.750 | 7.830 | 1.750 |
| Rmerge | 0.051 | 0.025 | 0.511 |
| Rmeas | 0.059 | 0.030 | 0.638 |
| Total number of observations | 371684 | ||
| Number of reflections | 100396 | 1089 | 7207 |
| <I/σ(I)> | 15.35 | 40.96 | 1.85 |
| Completeness [%] | 99.6 | 96.4 | 96.3 |
| Redundancy | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 16-20% PEG 3350, 0-0.1 mM Tris pH 8 and 0.3-0.4 M NaI |
