2DC4
Structure of PH1012 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 | 2005-11-22 |
Detector | MARRESEARCH |
Wavelength(s) | 1 |
Spacegroup name | P 32 |
Unit cell lengths | 53.123, 53.123, 111.147 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 26.560 - 1.650 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yem |
RMSD bond length | 0.005 |
RMSD bond angle | 1.400 |
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] | 46.010 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.085 | 0.402 |
Number of reflections | 40754 | |
<I/σ(I)> | 23.1 | 2.63 |
Completeness [%] | 96.5 | 78.5 |
Redundancy | 4.1 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.62 | 295 | 27.5w/w(%) PEG4000, 0.1M Mes, NaOH, pH 6.62, microbatch, temperature 295.0K |