3ASM
Crystal structure of Q54A mutant protein of Bst-RNase HIII
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-14 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 67.249, 109.106, 48.329 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.190 - 2.603 |
| R-factor | 0.20498 |
| Rwork | 0.204 |
| R-free | 0.23262 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2d0a |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.925 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.106 | 0.400 |
| Total number of observations | 240534 | |
| Number of reflections | 11445 | |
| <I/σ(I)> | 18.5 | 3.33 |
| Completeness [%] | 99.9 | 98.9 |
| Redundancy | 6.9 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.085M Tris-HCl pH 8.5, 0.17M lithium sulfate, 25.5% PEG 4000, 15% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
