2IC9
The Coiled-coil Domain (residues 1-93) Structure of the Sin Nombre Virus Nucleocapsid Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-12 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9002 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 85.774, 42.647, 57.996 |
Unit cell angles | 90.00, 121.11, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.257 |
Rwork | 0.247 |
R-free | 0.32800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ic6 chain A |
RMSD bond length | 0.029 |
RMSD bond angle | 2.444 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.039 | 0.248 |
Number of reflections | 12165 | |
<I/σ(I)> | 32.7 | 7.5 |
Completeness [%] | 98.8 | 99 |
Redundancy | 4 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.15 M potassium bromide, 0.1 M Tris-HCl, 34% PEG mono-methyl ether (PEG MME) 200, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |