1M1Z
BETA-LACTAM SYNTHETASE APO ENZYME
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-21 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.179, 97.469, 80.968 |
Unit cell angles | 90.00, 90.42, 90.00 |
Refinement procedure
Resolution | 24.000 * - 1.950 |
Rwork | 0.197 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jgt |
RMSD bond length | 0.007 |
RMSD bond angle | 23.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.000 * | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.051 * | 0.253 * |
Total number of observations | 690463 * | |
Number of reflections | 69211 * | |
<I/σ(I)> | 18.01 | |
Completeness [%] | 92.8 | 90 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 296 | Miller, M.T., (2001) Nature Struct. Biol., 8, 684. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris | 50 (mM) | pH7.5 |
3 | 1 | reservoir | PEG4000 | 7 (%(w/v)) | |
4 | 1 | reservoir | 200 (mM) | ||
5 | 1 | reservoir | glycerol | 7 (%(v/v)) | |
6 | 1 | reservoir | Tris | 80 (mM) | pH8.0 |