4YAH
Crystal Structure of the Methionine Binding Protein, MetQ
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 | 2014-01-23 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.650, 87.370, 112.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.490 - 1.600 |
R-factor | 0.1557 |
Rwork | 0.154 |
R-free | 0.18290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p99 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.208 |
Data scaling software | Aimless (0.2.17) |
Phasing software | PHASER (2.5.5) |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 24.490 | 24.490 | 1.640 |
High resolution limit [Å] | 1.600 | 7.160 | 1.600 |
Rmerge | 0.075 | 0.021 | 1.125 |
Number of reflections | 38555 | ||
<I/σ(I)> | 11.5 | ||
Completeness [%] | 98.4 | 96.7 | 96.1 |
Redundancy | 4.1 | 4.2 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 20% PEG 4000, 3% PEG 400, 200 mM Ammonium Acetate, 100 mM Sodium Citrate, pH 5.6 |