6LCN
Crystal structure of Serine Acetyltransferase from Planctomyces limnophilus at 2.15A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2017-10-14 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5417 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 84.719, 113.165, 230.133 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.596 - 2.150 |
Rwork | 0.187 |
R-free | 0.22300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3f1x |
RMSD bond length | 0.007 |
RMSD bond angle | 1.475 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.596 | 2.227 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.095 | 0.742 |
Rmeas | 0.108 | 0.841 |
Rpim | 0.050 | 0.391 |
Number of reflections | 120745 | 11863 |
<I/σ(I)> | 14.44 | |
Completeness [%] | 99.6 | 99.23 |
Redundancy | 4.7 | 4.5 |
CC(1/2) | 0.997 | 0.658 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 278 | 0.1M MES pH=6.5, 12% w/v PEG 20,000 |