5IDI
Structure of beta glucosidase 1A from Thermotoga neapolitana, mutant E349A
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 | 2011-04-12 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0402 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.277, 98.726, 154.756 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.17082 |
Rwork | 0.169 |
R-free | 0.21470 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cbv |
RMSD bond length | 0.027 |
RMSD bond angle | 2.240 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.100 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.084 | 1.172 |
Number of reflections | 81717 | |
<I/σ(I)> | 12.6 | 1.9 |
Completeness [%] | 99.1 | 85.4 |
Redundancy | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 5 | 288 | Protein at 12 mg/ml in 20 mM citrate phosphate buffer, pH 5.6. Hanging drops consisting of 1 microlitre of protein solution and 2 microlitres of reservoir solution (18-23% w/v PEG 6000, 0.2 M sodium chloride, 0.1 M sodium acetate, pH 5.0) equilibrated against 1 ml of reservoir solution. Rod-shaped crystals of approximate dimensions 0.3 x 0.2 x 0.3 mm grew after 8-10 days. |