6CVA
Crystal structure of the N. meningitides methionine-binding protein in its substrate-free conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-04-14 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.97946 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 52.564, 89.663, 45.088 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.223 - 1.559 |
R-factor | 0.1902 |
Rwork | 0.188 |
R-free | 0.22010 |
Structure solution method | SAD |
RMSD bond length | 0.003 |
RMSD bond angle | 0.681 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.31) |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 34.223 | 34.223 | 1.220 |
High resolution limit [Å] | 1.190 | 5.320 | 1.190 |
Rmerge | 0.111 | 0.059 | 4.884 |
Rmeas | 0.132 | 0.069 | 6.153 |
Total number of observations | 425726 | ||
Number of reflections | 128188 | 1512 | 7045 |
<I/σ(I)> | 4.23 | 17.15 | 0.15 |
Completeness [%] | 95.6 | 97.6 | 71 |
Redundancy | 3.321 | 3.438 | 2.55 |
CC(1/2) | 0.995 | 0.994 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.2M MgCl2, 0.1M Bis-Tris pH5.5, 25% PEG3350 |