2EEN
Structure of PH1819 protein from Pyrococcus Horikoshii OT3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-10-22 |
Detector | MARRESEARCH |
Wavelength(s) | 1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.394, 36.439, 80.375 |
Unit cell angles | 90.00, 91.80, 90.00 |
Refinement procedure
Resolution | 33.180 - 1.650 |
Rwork | 0.229 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dc4 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.180 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.049 | 0.344 |
Number of reflections | 44006 | |
<I/σ(I)> | 24.5 | 3.1 |
Completeness [%] | 98.4 | 99.8 |
Redundancy | 3.2 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 8.4 | 295 | 27.5w/w(%) PEG 4000, 0.1M TRIS-HCL, pH 8.4, microbatch, temperature 295.0K |