5F4Q
Crystal structure of the human egg surface protein Juno
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-28 |
| Detector | RIGAKU SATURN 92 |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 41 |
| Unit cell lengths | 73.150, 73.150, 163.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.680 - 1.800 |
| R-factor | 0.1985 |
| Rwork | 0.196 |
| R-free | 0.22660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5f4e |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.085 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.8) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.680 | 43.680 | 1.840 |
| High resolution limit [Å] | 1.800 | 9.180 | 1.800 |
| Rmerge | 0.117 | 0.025 | 0.735 |
| Rpim | 0.044 | 0.010 | 0.284 |
| Total number of observations | 640808 | 4586 | 34618 |
| Number of reflections | 79079 | ||
| <I/σ(I)> | 17.5 | 62.6 | 3 |
| Completeness [%] | 100.0 | 99.2 | 99.8 |
| Redundancy | 8.1 | 7.4 | 7.6 |
| CC(1/2) | 0.999 | 1.000 | 0.898 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | 0.02 M magnesium chloride, 0.1 M HEPES sodium salt [pH 7.5], 22% (w/v) Polyacrylic acid 5100 |






