4L0M
Crystal structure of a putative 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Borrelia burgdorferi B31 bound to Adenine (Target NYSGRC-029268 )
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-02-14 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.979310 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 48.083, 48.083, 241.838 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.120 - 1.700 |
| R-factor | 0.2286 |
| Rwork | 0.227 |
| R-free | 0.26690 |
| Structure solution method | SAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.522 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | SHELX (C) |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.630 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.100 | 2.210 |
| Number of reflections | 32546 | |
| <I/σ(I)> | 28.3 | 2.4 |
| Completeness [%] | 99.9 | 99.3 |
| Redundancy | 27.9 | 26.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | Protein (20mM HEPES pH7.5, 150mM NaCl, 5% glycerol, and 5mM DTT); Reservoir (MCSG2 #27: 0.2 M Ammonium Acetate, 0.1 M HEPES:NaOH pH 7.5, 25% (w/v) PEG 3350 ); Cryoprotection (33% Ethylene glycol), Sitting Drop, Vapor Diffusion, temperature 298K, VAPOR DIFFUSION, SITTING DROP |
