1V3Y
The crystal structure of peptide deformylase from Thermus thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-04-23 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.00 |
Spacegroup name | P 43 |
Unit cell lengths | 62.582, 62.582, 105.271 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.800 - 1.810 |
R-factor | 0.17271 |
Rwork | 0.171 |
R-free | 0.20849 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.018 |
RMSD bond angle | 1.617 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.19) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 19.960 |
High resolution limit [Å] | 1.810 |
Number of reflections | 36563 |
Completeness [%] | 99.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 288 | 20% PEG 4000, 0.1M Tris-HCl, 200MM Sodium Acetate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K |