3A1M
A fusion protein of a beta helix region of gene product 5 and the foldon region of bacteriophage T4
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-11-23 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 98.814, 57.010, 136.594 |
| Unit cell angles | 90.00, 103.90, 90.00 |
Refinement procedure
| Resolution | 29.170 - 2.000 |
| R-factor | 0.22492 |
| Rwork | 0.223 |
| R-free | 0.26827 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k28 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.100 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | X-PLOR |
| Refinement software | REFMAC (5.5.0063) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.034 | 0.106 |
| Number of reflections | 44791 | |
| <I/σ(I)> | 24.9 | 729 |
| Completeness [%] | 85.3 | 85.7 |
| Redundancy | 3.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | Ammonium sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
