3EER
High resolution structure of putative organic hydroperoxide resistance protein from Vibrio cholerae O1 biovar eltor str. N16961
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Detector technology | CCD |
Collection date | 2008-08-16 |
Detector | SBC-3 |
Spacegroup name | I 21 21 21 |
Unit cell lengths | 59.649, 71.127, 71.629 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.450 |
R-factor | 0.141 |
Rwork | 0.139 |
R-free | 0.16400 |
Structure solution method | SAD |
RMSD bond length | 0.015 |
RMSD bond angle | 1.508 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.480 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.106 | 0.464 |
Number of reflections | 27234 | |
<I/σ(I)> | 19.7 | 2.34 |
Completeness [%] | 99.1 | 90.9 |
Redundancy | 6.4 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 291 | 0.2 M ZnAcetate, 0.1 M Imidazole, 20% Peg 3000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |