3O2E
Crystal structure of a bol-like protein from babesia bovis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-20 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 66.300, 66.300, 35.290 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.530 - 1.950 |
R-factor | 0.185 |
Rwork | 0.183 |
R-free | 0.24100 |
Structure solution method | SAD |
Starting model (for MR) | iodide SAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.712 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.094 | 0.481 |
Number of reflections | 6133 | |
<I/σ(I)> | 19.39 | 4.4 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 18.3 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | EBS JCSG SCREEN E2: 2M AMMONIUM SULPHATE, 100MM CACODYLATE PH 6.5, 200MM NACL: BABOA.10365.A AT 12.4MG/ML, ENCUA.00735 AT 29.3MG/ML, PH N/A, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |