2WLQ
Nucleophile-disabled Lam16A mutant holds laminariheptaose (L7) in a cyclical conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-09-13 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.273, 47.910, 152.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.843 - 1.400 |
R-factor | 0.171 |
Rwork | 0.170 |
R-free | 0.19400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cl2 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.615 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SCALA |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.800 | 1.480 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.080 | 0.400 |
Number of reflections | 56288 | |
<I/σ(I)> | 16.6 | 3.3 |
Completeness [%] | 98.2 | 99.2 |
Redundancy | 6.3 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | 293 | 8 MG/ML PROTEIN SOLUTION IN 10 MM NAOAC WAS MIXED WITH AN EQUAL VOLUME OF CRYSTALLIZATION BUFFER CONTAINING 20% PEG 3350, 0.2 M AMMONIUM NITRATE AND 10 MM SODIUM ACETATE BUFFER, PH 5.0, AT 20 DEGREES. SOAKING: 24 H IN 5 MM LAMINAROHEPTASACCHARIDE. CRYOPROTECTANT CONTAINED 35 % (W/V) PEG 3350, 0.2 M AMMONIUM NITRATE AND 10 MM SODIUM ACETATE BUFFER, PH 5.0 |