1A5L
K217C VARIANT OF KLEBSIELLA AEROGENES UREASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1997-10 |
| Detector | XUONG-HAMLIN MULTIWIRE |
| Spacegroup name | I 21 3 |
| Unit cell lengths | 170.800, 170.800, 170.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| R-factor | 0.186 |
| Rwork | 0.186 |
| Structure solution method | DIFFERENCE FOURIER |
| RMSD bond length | 0.026 |
| RMSD bond angle | 25.060 * |
| Data reduction software | SDMS |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.280 | |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.091 * | 0.288 * |
| Number of reflections | 38169 | |
| <I/σ(I)> | 7.7 | 2.6 |
| Completeness [%] | 93.0 | 69 |
| Redundancy | 2 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 25 * | PROTEIN WAS CRYSTALLIZED FROM 100 MM HEPES, PH 7.5, 1.6 M LI2SO4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | urease | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | EDTA | 0.5 (mM) | |
| 4 | 1 | drop | beta-mercaptoethanol | 0.5 (mM) | |
| 5 | 1 | drop | 0.75-0.85 (M) | ||
| 6 | 1 | drop | HEPES | 50 (mM) | |
| 7 | 1 | reservoir | 1.5-1.7 (M) | ||
| 8 | 1 | reservoir | HEPES | 100 (mM) |
