1X3L
Crystal structure of the PH0495 protein from pyrococccus 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 | 2004-06-26 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.00 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 190.908, 52.895, 52.683 |
Unit cell angles | 90.00, 91.31, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.100 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1O0U |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.065 | 0.217 |
Number of reflections | 30781 | |
<I/σ(I)> | 15.7 | 3.41 |
Completeness [%] | 99.3 | 97.1 |
Redundancy | 4.01 | 3.79 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 4.6 | 295 | ammonium sulfate, acetate, pH 4.6, microbatch, temperature 295K |