1VLR
Crystal structure of mRNA decapping enzyme (DcpS) from Mus musculus at 1.83 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-08 |
Detector | ADSC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 65.399, 59.231, 100.140 |
Unit cell angles | 90.00, 103.80, 90.00 |
Refinement procedure
Resolution | 37.580 - 1.830 |
R-factor | 0.16053 |
Rwork | 0.158 |
R-free | 0.20101 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1st0 |
RMSD bond length | 0.018 |
RMSD bond angle | 1.667 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0001) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.580 | 1.900 |
High resolution limit [Å] | 1.830 | 1.830 |
Number of reflections | 64852 | |
<I/σ(I)> | 18.07 | 3.04 |
Completeness [%] | 97.9 | 84.84 |
Redundancy | 3.69 | 3.07 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION,SITTING DROP,NANODROP | 7.2 | 277 | 0.2M KF, 20.0% PEG-3350, No Buffer pH 7.2, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K |