4C7F
Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 120 |
Collection date | 2011-07-23 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.790, 129.240, 149.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 97.890 - 2.000 |
R-factor | 0.15848 |
Rwork | 0.156 |
R-free | 0.19712 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4c7d |
RMSD bond length | 0.019 |
RMSD bond angle | 1.855 |
Data reduction software | XDS |
Data scaling software | SCALA |
Refinement software | REFMAC (5.8.0033) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.950 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.180 | 0.530 |
Number of reflections | 95616 | |
<I/σ(I)> | 8.8 | 3.2 |
Completeness [%] | 99.4 | 98.6 |
Redundancy | 5.6 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.1 M BIS-TRIS PH 6.5, 4 % (W/V) PEG 6000, 5 % DMSO |