5H4G
Structure of PIN-domain protein (VapC4 toxin) from Pyrococcus horikoshii determined at 1.77 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 300 |
Detector technology | CCD |
Collection date | 2011-03-14 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97625 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.780, 44.640, 52.370 |
Unit cell angles | 90.00, 103.40, 90.00 |
Refinement procedure
Resolution | 50.940 - 1.770 |
R-factor | 0.17001 |
Rwork | 0.167 |
R-free | 0.22135 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1v96 |
RMSD bond length | 0.020 |
RMSD bond angle | 1.899 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.940 | 1.810 |
High resolution limit [Å] | 1.770 | 1.770 |
Rmerge | 0.749 | |
Number of reflections | 22115 | |
<I/σ(I)> | 18.4 | 2.3 |
Completeness [%] | 99.1 | 97.1 |
Redundancy | 7.2 | 6.2 |
CC(1/2) | 0.680 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295 | 0.2M Sodium acetate trihydrate, 0.1M Tris-HCl, 30%(w/v) PEG 4000, 0.1M Turine |