3B7A
Complex of S52A Substituted Droposphila LUSH protein with Ethanol
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Detector technology | CCD |
Collection date | 2004-07-15 |
Detector | NOIR-1 |
Wavelength(s) | 1.12 |
Spacegroup name | P 43 |
Unit cell lengths | 46.873, 46.873, 111.206 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.202 |
Rwork | 0.198 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ooh |
RMSD bond length | 0.009 |
RMSD bond angle | 1.074 |
Data reduction software | d*TREK |
Data scaling software | d*TREK (9.2LDz) |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.760 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.070 | 0.462 |
Number of reflections | 25896 | |
<I/σ(I)> | 8.4 | 2.3 |
Completeness [%] | 98.9 | 99.8 |
Redundancy | 3.35 | 2.91 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 295 | 25% PEG 4000, 100mM Sodium Acetate, 3:1 protein/well solution, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K |