1WS1
Structure analysis of peptide deformylase from Bacillus cereus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-05-10 |
Detector | BRUKER PROTEUM 300 |
Wavelength(s) | 1.12714 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.310, 44.558, 84.474 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.620 - 2.000 |
R-factor | 0.223 |
Rwork | 0.184 |
R-free | 0.23700 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.023 |
RMSD bond angle | 2.600 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.620 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 10263 | |
Completeness [%] | 92.3 | 58.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 295 | MES, PEG6000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |