5HK8
Crystal structure of a methylesterase protein MES16 from Arabidopsis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-01-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.979 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 149.642, 176.362, 168.445 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.000 - 2.800 |
R-factor | 0.208 |
Rwork | 0.206 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xkl |
RMSD bond length | 0.005 |
RMSD bond angle | 0.910 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.065 | 0.676 |
Number of reflections | 54972 | |
<I/σ(I)> | 9.8 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.7 | 15.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | Sodium acetate trihydrate, PEG 4000, isopropanol |