7QXV
Crystal Structure of Haem-Binding Protein HemS Mutant F104A F199A, from Yersinia enterocolitica
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-05-01 |
Detector | DECTRIS EIGER2 X 16M |
Wavelength(s) | 0.9793 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.028, 69.613, 73.766 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.570 - 1.670 |
R-factor | 0.235 |
Rwork | 0.233 |
R-free | 0.28100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2j0p |
RMSD bond length | 0.008 |
RMSD bond angle | 1.459 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.570 | 50.590 | 1.700 |
High resolution limit [Å] | 1.670 | 4.530 | 1.670 |
Rmeas | 0.415 | 0.082 | 93.925 |
Rpim | 0.096 | 0.020 | 22.135 |
Total number of observations | 701834 | 35283 | 32887 |
Number of reflections | 37692 | 2068 | 1840 |
<I/σ(I)> | 5.6 | 32.7 | 0.2 |
Completeness [%] | 100.0 | 100 | 100 |
Redundancy | 18.6 | 17.1 | 17.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 100 mM tris-HCl 1.8 M (NH4)2SO4, 2% (w/v) PEG 400 |