2R6I
Crystal structure of Atu1473 protein, a putative chaperone from Agrobacterium tumefaciens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-02 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97920 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 86.304, 108.107, 142.393 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.800 - 2.590 |
R-factor | 0.24226 |
Rwork | 0.240 |
R-free | 0.28943 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.678 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SHELXD |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.800 | 2.690 |
High resolution limit [Å] | 2.590 | 2.590 |
Rmerge | 0.152 | 0.841 |
Number of reflections | 21099 | |
<I/σ(I)> | 23.8 | 3.51 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.5 | 13.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 0.1M Hepes pH 7.5, 0.2M NH4(OAC), 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 294K |