5ZDI
Crystal structure of CsaA chaperone protein from picrophilus torridus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | Cu FINE FOCUS |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2015-12-16 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.009, 65.334, 75.588 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.430 - 1.700 |
R-factor | 0.18496 |
Rwork | 0.183 |
R-free | 0.22361 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2nzh |
RMSD bond length | 0.022 |
RMSD bond angle | 2.027 |
Data scaling software | HKL-2000 |
Phasing software | PHASER (2.6.1) |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 25764 | |
<I/σ(I)> | 24.96 | |
Completeness [%] | 98.0 | |
Redundancy | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 20mM Tris buffer pH 8.0, 0.2 M ammonium sul-phate, 1 M NaCl, 25% PEG 8000 |