6W78
crystal structure of a plant ice-binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-10-31 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.978 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.895, 57.453, 135.538 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.414 - 2.311 |
Rwork | 0.162 |
R-free | 0.22280 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ogq |
RMSD bond length | 0.014 |
RMSD bond angle | 2.047 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.360 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.127 | 0.491 |
Number of reflections | 13160 | 690 |
<I/σ(I)> | 18 | |
Completeness [%] | 99.8 | |
Redundancy | 8.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 291 | 0.2 M sodium malonate (pH 4.0), and 20% w/v polyethylene glycol 3,350 |