2XI5
N-terminal endonuclease domain of La Crosse virus L-protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-31 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 124.200, 124.200, 294.320 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.160 - 2.200 |
R-factor | 0.193 |
Rwork | 0.192 |
R-free | 0.22400 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.018 |
RMSD bond angle | 1.547 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | autoSHARP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.080 | 0.590 |
Number of reflections | 65657 | |
<I/σ(I)> | 23.5 | 4.2 |
Completeness [%] | 95.4 | 95.7 |
Redundancy | 11.1 | 10.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 15-20 MG PER ML PROTEIN IN 20 MM HEPES 150 MM NACL 5MM MNCL2 AND 2.5 MM BETA-MERCAPTO-ETHANOL AT PH 7.5 AND A RESERVOIR COMPOSITION OF 3.4 M NA-FORMATE 0.1 M TRIS-HCL PH 8 |