2HDB
HMG-CoA synthase from Enterococcus faecalis. Mutation alanine 110 to glycine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-ID-B |
Synchrotron site | APS |
Beamline | 14-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-20 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.24 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 105.310, 109.690, 141.850 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.920 - 2.200 |
R-factor | 0.192 |
Rwork | 0.192 |
R-free | 0.22100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HMG-CoA Synthase native structure from Enterococcus faecalis PDB 1X9E. |
RMSD bond length | 0.007 |
RMSD bond angle | 1.400 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 41829 | |
<I/σ(I)> | 26.4 | 6.4 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.4 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 290 | 2.2M ammonium sulfate, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 290K |