3FFP
X ray structure of the complex between carbonic anhydrase II and LC inhibitors
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OXFORD DIFFRACTION ENHANCED ULTRA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-09-09 |
Detector | OXFORD SAPPHIRE CCD |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.180, 41.430, 72.240 |
Unit cell angles | 90.00, 104.47, 90.00 |
Refinement procedure
Resolution | 11.830 - 1.810 |
R-factor | 0.18948 |
Rwork | 0.187 |
R-free | 0.24018 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ca2 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.595 |
Data reduction software | CrysalisPro (Oxford Diffraction2006) |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.000 | 1.870 |
High resolution limit [Å] | 1.810 | 1.810 |
Number of reflections | 22187 | |
<I/σ(I)> | 20.9 | 3.08 |
Completeness [%] | 99.6 | 100 |
Redundancy | 4.2 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 100mM Tris-HCl PH 7.7-7.8, 2mM sodium 4-(hydroxymercury)benzoate, VAPOR DIFFUSION, HANGING DROP, temperature 277K |