27AE
Crystal structure of protein PF1862 from Pyrococcus furiosus crystallized at 21 degree Celsius
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2026-02-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.997 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.768, 42.120, 66.807 |
| Unit cell angles | 90.00, 106.26, 90.00 |
Refinement procedure
| Resolution | 37.780 - 1.900 |
| R-factor | 0.1912 |
| Rwork | 0.189 |
| R-free | 0.23040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AlphaFold |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.558 |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.120 | 1.940 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.070 | 0.896 |
| Rmeas | 0.075 | 0.974 |
| Rpim | 0.028 | 0.375 |
| Number of reflections | 16953 | 1052 |
| <I/σ(I)> | 17.7 | 2.1 |
| Completeness [%] | 99.9 | 98.4 |
| Redundancy | 7.4 | 6.6 |
| CC(1/2) | 0.999 | 0.753 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.5 | 294 | 0.1 M Bis-Tris (pH 5.5) and 17% PEG 10000; protein PF1862 at 40 mg/mL |
