1SPP
THE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAIN
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 285 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-11 |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 96.370, 96.370, 71.320 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.400 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| R-free | 0.25900 |
| Structure solution method | MIR |
| RMSD bond length | 0.009 |
| RMSD bond angle | 28.390 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((ROTAVATA)) |
| Phasing software | CCP4 |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.940 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.057 | 0.265 * |
| Total number of observations | 61270 * | |
| Number of reflections | 14809 | |
| <I/σ(I)> | 7.1 | 3 |
| Completeness [%] | 97.0 | 98.4 |
| Redundancy | 4.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | 22 * | PROTEIN WAS CRYSTALLIZED FROM 30% (W/V) PEG 2000, 100 MM AMMONIUM ACETATE, PH 6.5. THE INITIAL PROTEIN CONCENTRATION WAS 15 MG/ML |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | sodium phosphate | 50 (mM) | |
| 3 | 1 | reservoir | PEG2000 | 30 (%(w/v)) | |
| 4 | 1 | reservoir | ammonium acetate | 0.1 (M) |
