3AH6
Remarkable improvement of the heat stability of CutA1 from E.coli by rational protein designing
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-01 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.239, 96.872, 106.352 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.230 - 2.400 |
R-factor | 0.202 |
Rwork | 0.202 |
R-free | 0.25100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3aa8 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.062 | 0.300 |
Number of reflections | 25891 | |
<I/σ(I)> | 6.52 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 7 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.1 M HEPS (pH 7.5) including 1.4 M tri-sodium citrate dihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 20K, temperature 293K |