6SZ5
Human calmodulin bound to a peptide of human NADPH oxidase 5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-01 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 1.07227 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 24.759, 60.840, 102.444 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.210 - 2.230 |
| R-factor | 0.2227 |
| Rwork | 0.219 |
| R-free | 0.29370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5k8q |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.417 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.6.3) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 39.210 | 39.180 | 2.310 |
| High resolution limit [Å] | 2.230 | 8.640 | 2.230 |
| Rmerge | 0.201 | 0.063 | 1.469 |
| Rmeas | 0.220 | 0.070 | 1.600 |
| Rpim | 0.088 | 0.030 | 0.628 |
| Total number of observations | 909 | 4738 | |
| Number of reflections | 8098 | 177 | 754 |
| <I/σ(I)> | 6.5 | 19.5 | 1.1 |
| Completeness [%] | 99.9 | 99.2 | 100 |
| Redundancy | 6 | 5.1 | 6.3 |
| CC(1/2) | 0.992 | 0.995 | 0.529 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 293 | 30 mM Tris-HCl at pH 7.4, 2.5 mM CaCl2 and 2.5% (v/v) glycerol |
