5TV2
Crystal structure of a fragment (1-405) of an elongation factor G from Vibrio vulnificus CMCP6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-05 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.678, 54.496, 65.319 |
Unit cell angles | 90.00, 116.58, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.600 |
R-factor | 0.18232 |
Rwork | 0.179 |
R-free | 0.25307 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fn5 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.782 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.630 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.050 | 0.730 |
Number of reflections | 48492 | |
<I/σ(I)> | 31.3 | 2.1 |
Completeness [%] | 97.8 | 100 |
Redundancy | 6.4 | 4.3 |
CC(1/2) | 0.750 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | 0.1 MMT buffer, 25 % PEG 1500 |