3MGK
CRYSTAL STRUCTURE OF PROBABLE PROTEASE/AMIDASE FROM Clostridium acetobutylicum ATCC 824
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2010-03-28 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 151.539, 70.354, 40.195 |
Unit cell angles | 90.00, 101.18, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.1884 |
Rwork | 0.186 |
R-free | 0.24326 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.321 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELX |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 28333 | |
<I/σ(I)> | 9 | 1.3 |
Completeness [%] | 99.5 | 95.8 |
Redundancy | 3.2 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 0.1M BIS-TRIS, PH 6.5, 25% PEG3350, 200MM AMMONIUM ACETATE, 10% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K |