6IV3
Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation W252A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-11-20 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 113.461, 159.607, 162.674 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 66.106 - 2.515 |
R-factor | 0.2341 |
Rwork | 0.234 |
R-free | 0.26470 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.055 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 66.110 | 2.610 |
High resolution limit [Å] | 2.520 | 2.520 |
Number of reflections | 99774 | |
<I/σ(I)> | 12.75 | |
Completeness [%] | 98.7 | |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.05M zinc acetate, 6% v/v ethylene glycol, 0.1M sodium cacodylate, pH 6.0, 6.6% w/v PEG 8000 |