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 |
