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 |
