1A5O
K217C VARIANT OF KLEBSIELLA AEROGENES UREASE, CHEMICALLY RESCUED BY FORMATE AND NICKEL
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1997-12 |
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 - 2.500 |
R-factor | 0.181 |
Rwork | 0.181 |
Structure solution method | DIFFERENCE FOURIER |
RMSD bond length | 0.009 |
RMSD bond angle | 25.040 * |
Data reduction software | SDMS |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 2.590 | |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.117 * | 0.393 * |
Number of reflections | 27738 | |
<I/σ(I)> | 9.996 | 2.9 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.1 | 2.8 |
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; THEN CRYSTAL WAS SOAKED IN 100 MM HEPES, 500MM FORMATE, PH 7.5, 2.0 M LI2SO4, 1.5 MM NICL2 |
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) |