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 |
