7KR9
Bifunctional enzyme GlmU bound to Zn(II)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-06-01 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9537 |
Spacegroup name | H 3 2 |
Unit cell lengths | 92.872, 92.872, 280.703 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.830 - 1.900 |
R-factor | 0.18721 |
Rwork | 0.185 |
R-free | 0.22697 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hm8 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.551 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.000 | 1.940 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 37206 | 2319 |
<I/σ(I)> | 18.2 | |
Completeness [%] | 99.9 | |
Redundancy | 10.3 | |
CC(1/2) | 0.999 | 0.943 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 293 | 20 mM Tris-HCL, pH 7.2, 20% (v/v) PEG 400, 50 mM NaCl, 300 mM CaCl2, and 1 mM ZnCl2 |