5KKF
Crystal structure of TEM1 beta-lactamase mutant I263L
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL14-1 |
Synchrotron site | SSRL |
Beamline | BL14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-05-18 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 1.181 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.500, 84.030, 94.920 |
Unit cell angles | 90.00, 90.42, 90.00 |
Refinement procedure
Resolution | 51.190 - 1.820 |
R-factor | 0.185 |
Rwork | 0.182 |
R-free | 0.22700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5hvi |
RMSD bond length | 0.011 |
RMSD bond angle | 1.135 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless (0.5.17) |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 62.920 | 1.850 |
High resolution limit [Å] | 1.820 | 1.820 |
Rmerge | 0.130 | 0.444 |
Number of reflections | 82018 | |
<I/σ(I)> | 6.3 | |
Completeness [%] | 96.5 | 94.8 |
Redundancy | 3.8 | 3.8 |
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 |