5XCT
Crystal structure of P20.1 Fv-clasp fragment with its antigen peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-09-21 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.100, 55.159, 62.484 |
| Unit cell angles | 90.00, 93.16, 90.00 |
Refinement procedure
| Resolution | 27.579 - 1.170 |
| R-factor | 0.1536 |
| Rwork | 0.152 |
| R-free | 0.18490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5xcq |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.929 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((dev_2341: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.190 |
| High resolution limit [Å] | 1.170 | 1.170 |
| Number of reflections | 109121 | |
| <I/σ(I)> | 17.77 | 2.45 |
| Completeness [%] | 97.0 | 89.4 |
| Redundancy | 4.2 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 0.1M Bis-Tris (pH 6.5), 20%(w/v) PEG3350 |
