1H5V
Thiopentasaccharide complex of the endoglucanase Cel5A from Bacillus agaradharens at 1.1 A resolution in the tetragonal crystal form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-03-15 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 75.169, 75.169, 135.471 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.100 |
R-factor | 0.12 * |
Rwork | 0.120 |
R-free | 0.13800 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qhz |
RMSD bond length | 0.017 * |
RMSD bond angle | 1.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.140 |
High resolution limit [Å] | 1.100 | 1.100 |
Rmerge | 0.055 | 0.288 |
Number of reflections | 155682 | |
<I/σ(I)> | 20.6 | 4.2 |
Completeness [%] | 99.5 | 98.7 |
Redundancy | 3.6 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7 | PROTEIN (20MGML-1) WAS CRYSTALLISED FROM 28% PEG400 AS PRECIPITANT, 100MM HEPES AT PH 7.0 AS BUFFER AND 200 MM CACL2. THE PROTEIN WAS INCUBATED WITH THE 1MM OF SUBSTRATE FOR AN HOUR PRIOR TO COCRYSTALLISATIOM |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG400 | 28-30 (%(v/v)) | |
2 | 1 | reservoir | tri-ethanolamine | 100 (mM) | or HEPES pH7.0 |
3 | 1 | reservoir | 200 (mM) |