1XS0
Structure of the E. coli Ivy protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-30 |
Detector | MARRESEARCH |
Wavelength(s) | 0.97917, 0.97941, 0.97393 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 81.339, 46.962, 88.044 |
Unit cell angles | 90.00, 89.95, 90.00 |
Refinement procedure
Resolution | 14.520 - 1.580 |
R-factor | 0.225 |
Rwork | 0.225 |
R-free | 0.26000 |
Structure solution method | MAD |
RMSD bond length | 0.025 |
RMSD bond angle | 2.200 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.700 | 1.670 |
High resolution limit [Å] | 1.580 | 1.580 |
Number of reflections | 44577 | |
<I/σ(I)> | 3.1 | |
Completeness [%] | 98.1 | 98.1 |
Redundancy | 3 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.75 | 293 | 1.4M sodium citrate, 8% PEG 8000, 20mM TRIS, 50mM NaCl, pH 6.75, VAPOR DIFFUSION, HANGING DROP, temperature 293K |