3E3I
H. influenzae beta-carbonic anhydrase, variant G41A with 100 mM bicarbonate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F2 |
| Synchrotron site | CHESS |
| Beamline | F2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-14 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.980 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 229.593, 144.437, 104.891 |
| Unit cell angles | 90.00, 94.43, 90.00 |
Refinement procedure
| Resolution | 29.750 - 2.000 |
| R-factor | 0.203 |
| Rwork | 0.201 |
| R-free | 0.23600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2a8d |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.192 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 122.169 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.055 | 0.475 |
| Total number of observations | 57681 | |
| Number of reflections | 205440 | |
| <I/σ(I)> | 19.1 | 1.9 |
| Completeness [%] | 89.6 | 55.6 |
| Redundancy | 4.8 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.1 M HEPES, 1.8 M ammonium sulfate, 4% PEG 400, 100 mM sodium bicarbonate, 12 mg/mL protein, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
