2X3M
Crystal Structure of Hypothetical Protein ORF239 from Pyrobaculum Spherical Virus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-03-21 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 42.898, 53.715, 95.193 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.560 - 1.450 |
R-factor | 0.178 |
Rwork | 0.177 |
R-free | 0.19500 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.006 |
RMSD bond angle | 0.916 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.6.0079) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 1.500 | 1.500 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.040 | 0.460 |
Number of reflections | 39560 | |
<I/σ(I)> | 28.3 | 1.8 |
Completeness [%] | 97.0 | 73 |
Redundancy | 4.4 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 20% PEG 3350, 0.2M POTASSIUM ACETATE CRYOPROTECTION WITH 20% PEG 400 |