3VZI
Crystal Structure of CRISPR-associated Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-03-17 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.973, 54.842, 179.356 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.660 |
R-factor | 0.21014 |
Rwork | 0.206 |
R-free | 0.28674 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3kg4 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.488 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.740 |
High resolution limit [Å] | 2.650 | 2.650 |
Number of reflections | 13585 | |
Completeness [%] | 99.8 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 25% PEG3350, 0.1M DL-malic acid, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |