5HVI
Crystal structure of TEM1 beta-lactamase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-06 |
Detector | NOIR-1 |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.663, 84.156, 95.703 |
Unit cell angles | 90.00, 90.07, 90.00 |
Refinement procedure
Resolution | 63.198 - 1.640 |
R-factor | 0.1693 |
Rwork | 0.167 |
R-free | 0.20650 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1btl |
RMSD bond length | 0.008 |
RMSD bond angle | 1.132 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.1) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 63.200 | 1.670 |
High resolution limit [Å] | 1.640 | 1.640 |
Rmerge | 0.061 | 0.334 |
Rpim | 0.037 | |
Total number of observations | 409738 | |
Number of reflections | 113836 | |
<I/σ(I)> | 15.1 | 3.4 |
Completeness [%] | 96.9 | 89.6 |
Redundancy | 3.6 | 3.4 |
CC(1/2) | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 294 | 2% (v/v) tacsimate (pH 6.0), 0.1 M Bis-Tris (pH 6.5), 20% (w/v) PEG 3350 |