2ZTI
Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes
Replaces: 2EHKExperimental 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 | IMAGE PLATE |
Collection date | 2006-11-04 |
Detector | RIGAKU |
Wavelength(s) | 1.0 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 76.282, 76.282, 82.585 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 2.600 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1v7r |
RMSD bond length | 0.008 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.070 | |
Number of reflections | 8881 | |
<I/σ(I)> | 9.2 | |
Completeness [%] | 99.8 | 97.3 |
Redundancy | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 295 | 0.08M MES, 1.6M NH(2)SO4, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K |