2H15
Carbonic anhydrase inhibitors: Clashing with Ala65 as a means of designing isozyme-selective inhibitors that show low affinity for the ubiquitous isozyme II
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OXFORD DIFFRACTION ENHANCE ULTRA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-23 |
Detector | OXFORD SAPPHIRE CCD |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.150, 41.550, 72.250 |
Unit cell angles | 90.00, 104.23, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.240 |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.080 | 0.211 |
Number of reflections | 18403 | |
<I/σ(I)> | 10.8 | |
Completeness [%] | 98.5 | 81 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 278 | Tris-HCl pH 7.7-7.8, sodium 4-(hydroxymercury)benzoate, VAPOR DIFFUSION, HANGING DROP, temperature 278K |