1KH8
Structure of a cis-proline (P114) to glycine variant of Ribonuclease A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS II |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 40.870, 40.870, 129.250 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
Rwork | 0.195 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | High Salt Wild Type RNase A (PAUL: Kim et al Biochemistry 1992 31 12304-12314) |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.053 * | |
Number of reflections | 7592 * | |
Completeness [%] | 94.7 | 82.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.6 | 303 | NaPO4, CsCl2, ammonium sulfate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 303K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 5 (mg/ml) | |
2 | 1 | 1 | 0.15 (M) | ||
3 | 1 | 1 | 3 (M) | pH6.6 | |
4 | 1 | 2 | ammonium sulfate | 30 (%sat) |