2WNE
Mutant Laminarinase 16A cyclizes laminariheptaose
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-2 |
Synchrotron site | MAX II |
Beamline | I911-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-05-16 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.175, 47.911, 152.766 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.589 - 2.124 |
R-factor | 0.163 |
Rwork | 0.160 |
R-free | 0.22000 |
Structure solution method | OTHER |
Starting model (for MR) | NONE |
RMSD bond length | 0.014 |
RMSD bond angle | 1.477 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | REFMAC |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.900 | 2.200 |
High resolution limit [Å] | 2.110 | 2.100 |
Rmerge | 0.090 | 0.240 |
Number of reflections | 16720 | |
<I/σ(I)> | 12 | 5 |
Completeness [%] | 97.0 | 81 |
Redundancy | 3.6 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | HANGING DROP: 1 UL 2MG/ML PROTEIN MIXED WITH 1 UL RESERVOIR SOLUTION: 20% PEG 3350, 0.2 M NH4NO3 PH 5 (REERVOIR VOLUME 500 UL). XTALS WERE SOAKED O/N IN DROP OF 10 MM AL7F AND EQUAL VOLUME 35% PEG, 0.2 M NH4NO3 PH 5. |