3LIS
Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I (Monoclinic form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-04-07 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.010, 29.530, 64.380 |
Unit cell angles | 90.00, 101.91, 90.00 |
Refinement procedure
Resolution | 31.500 - 2.000 |
R-factor | 0.209 |
Rwork | 0.207 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.061 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.9) |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.276 | |
Number of reflections | 12439 | |
<I/σ(I)> | 11.7 | 4.1 |
Completeness [%] | 99.2 | 99.7 |
Redundancy | 3.3 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 289 | 0.1M malate-MES-Tris (MMT), 20% PEG 1500, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K |