5B01
Structure of a prenyltransferase in its unbound form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-01-14 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | P 41 |
Unit cell lengths | 106.604, 106.604, 310.713 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 3.450 |
Rwork | 0.225 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5b00 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 3.570 |
High resolution limit [Å] | 3.450 | 3.450 |
Rmerge | 0.113 | 0.492 |
Number of reflections | 44521 | |
<I/σ(I)> | 12.7 | 3.3 |
Completeness [%] | 98.4 | 100 |
Redundancy | 3.8 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.1 | 298 | 0.2M Na2HPO4, 16% PEG 3350 |