3LFP
Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I
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 | 2009-10-26 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | F 41 3 2 |
Unit cell lengths | 137.370, 137.370, 137.370 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.240 - 2.000 |
R-factor | 0.178 |
Rwork | 0.176 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y7y |
RMSD bond length | 0.023 |
RMSD bond angle | 1.753 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.072 | 0.408 |
Number of reflections | 7753 | 1052 |
<I/σ(I)> | 42.78 | 11.3 |
Completeness [%] | 97.2 | 94.2 |
Redundancy | 38.7 | 38.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | 0.1M Na HEPES, 1.4M Tri-sodium citrate dihydrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |