3FYA
Crystal Structure of an R35A mutant of the Restriction-Modification Controller Protein C.Esp1396I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-06 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9330 |
| Spacegroup name | P 65 |
| Unit cell lengths | 48.435, 48.435, 135.780 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.690 - 3.000 |
| R-factor | 0.249 |
| Rwork | 0.248 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3clc |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.690 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.959 | 41.920 | 3.110 |
| High resolution limit [Å] | 2.952 | 9.330 | 2.950 |
| Rmerge | 0.263 | 0.104 | 0.412 |
| Total number of observations | 1040 | 3041 | |
| Number of reflections | 3839 | ||
| <I/σ(I)> | 1.394 | 4.3 | 1.9 |
| Completeness [%] | 100.0 | 98.9 | 100 |
| Redundancy | 7.6 | 8 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | precipitation | 8 | 277 | 150 mM NaCl, 40 mM Tris-HCl, 5 % w/v glycerol, 2.5 mM CaCl2, pH 8.0, precipitation, temperature 277K |
