5IFP
STRUCTURE OF BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALBA BEAMLINE XALOC |
Synchrotron site | ALBA |
Beamline | XALOC |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-09-26 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97948 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 85.570, 111.421, 126.730 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 83.680 - 1.710 |
R-factor | 0.15127 |
Rwork | 0.150 |
R-free | 0.17136 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4iug |
RMSD bond length | 0.006 |
RMSD bond angle | 1.272 |
Data reduction software | MOSFLM (7.0.9) |
Data scaling software | Aimless (0.5.21) |
Phasing software | MOLREP (11.4.04) |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 83.680 | 1.740 |
High resolution limit [Å] | 1.710 | 1.710 |
Rmerge | 0.115 | 0.599 |
Number of reflections | 131079 | |
<I/σ(I)> | 11.5 | 3.7 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 6.8 | 6.2 |
CC(1/2) | 0.997 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 21% (W/V) PEG 3350, 0.1M BIS-TRIS BUFFER PH 5.5 , 0.2M LITHIUM SULPHATE |