5XCV
Crystal structure of NZ-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 | C 1 2 1 |
Unit cell lengths | 145.617, 50.122, 121.868 |
Unit cell angles | 90.00, 110.46, 90.00 |
Refinement procedure
Resolution | 41.762 - 2.143 |
R-factor | 0.2307 |
Rwork | 0.228 |
R-free | 0.27660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5xct 4yo0 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.904 |
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 | 2.180 |
High resolution limit [Å] | 2.140 | 2.140 |
Number of reflections | 46235 | |
<I/σ(I)> | 16.05 | 3.39 |
Completeness [%] | 99.6 | 99 |
Redundancy | 4.1 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 0.2M Calcium acetate, 0.1M MES (pH 6.5), 20%(w/v) PEG8000 |