4MAD
Crystal structure of beta-galactosidase C (BgaC) from Bacillus circulans ATCC 31382
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-04-09 |
Detector | BRUKER SMART 6500 |
Wavelength(s) | 0.9 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 143.268, 93.122, 119.567 |
Unit cell angles | 90.00, 125.67, 90.00 |
Refinement procedure
Resolution | 41.660 - 1.800 |
R-factor | 0.1829 |
Rwork | 0.181 |
R-free | 0.21560 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3d3a |
RMSD bond length | 0.008 |
RMSD bond angle | 1.051 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (refmac_5.5.0109) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
Rmerge | 0.109 | 0.066 | 0.520 |
Number of reflections | 117585 | ||
<I/σ(I)> | 24.672 | ||
Completeness [%] | 99.6 | 99.1 | 99.5 |
Redundancy | 10.5 | 10.4 | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 10mg/ml Protein in 10mM Tris-HCl and 1mM EDTA (pH 7.5), Reservoir (20% (w/v) PEG 6000, 100mM HEPES, 0.2M NaCl, pH 7.0), Protein:Reservoir=1:1 , VAPOR DIFFUSION, SITTING DROP, temperature 277K |