3K4T
Crystal structure of the virion-associated protein P3 from caulimovirus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-02-20 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.302, 28.818, 75.957 |
Unit cell angles | 90.00, 92.08, 90.00 |
Refinement procedure
Resolution | 18.980 - 2.590 |
R-factor | 0.223 |
Rwork | 0.219 |
R-free | 0.28900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3f6n |
RMSD bond length | 0.010 |
RMSD bond angle | 1.255 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.980 | 2.740 |
High resolution limit [Å] | 2.590 | 2.590 |
Rmerge | 0.074 | 0.302 |
Number of reflections | 9317 | |
<I/σ(I)> | 14.4 | 3.6 |
Completeness [%] | 96.1 | 99.2 |
Redundancy | 4.3 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 291 | 25% PEG 1000, 0.1M MES-NAOH BUFFER, 1.2 MOLAR-EXCESS DNA OLIGONUCLEOTIDE (POLY-AT, 14 BP) , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |