6BDY
Crystal Structure of the MetH Reactivation Domain bound to Sinefungin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-08-12 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9786 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.350, 61.577, 139.877 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.553 - 1.512 |
R-factor | 0.1458 |
Rwork | 0.144 |
R-free | 0.18590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | pdbid 1MSK |
RMSD bond length | 0.010 |
RMSD bond angle | 1.042 |
Data scaling software | HKL-2000 |
Phasing software | PHASER (2.6.0) |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.530 |
High resolution limit [Å] | 1.500 | 4.070 | 1.500 |
Rmerge | 0.061 | 0.037 | 0.280 |
Rmeas | 0.067 | 0.041 | 0.315 |
Rpim | 0.027 | 0.017 | 0.140 |
Total number of observations | 302238 | ||
Number of reflections | 51658 | 2687 | 2269 |
<I/σ(I)> | 13.7 | ||
Completeness [%] | 98.5 | 93.7 | 87.7 |
Redundancy | 5.9 | 5.5 | 4.5 |
CC(1/2) | 0.998 | 0.959 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 293 | 28% PEG 6000, 100mM Tris pH 7.3, 300mM magnesium acetate:15mg/mL protein, 3mM sinefungin, 10mM Tris 7.2, 10mM EDTA, 2:2uL |