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 | 






