3C2U
Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 5ID-B |
| Synchrotron site | APS |
| Beamline | 5ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-19 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9784, 0.9786, 0.9632 |
| Spacegroup name | P 1 |
| Unit cell lengths | 77.579, 84.401, 94.039 |
| Unit cell angles | 67.84, 81.31, 75.08 |
Refinement procedure
| Resolution | 87.040 - 1.300 |
| R-factor | 0.13572 |
| Rwork | 0.134 |
| R-free | 0.16303 |
| Structure solution method | MAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.656 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | SnB |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.240 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.063 | 0.382 |
| Number of reflections | 630354 | |
| <I/σ(I)> | 12.55 | 3.65 |
| Completeness [%] | 94.5 | 91.4 |
| Redundancy | 4.48 | 3.89 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 4 L of protein solution (1.6 mg/mL in 0.1 M BTP-HCl pH 8.0) mixed with 1 L of the well solution containing 22-25% (w/v) PEG 1100 monomethyl ether in 0.1M BTP-HCl, pH 8.0., VAPOR DIFFUSION, HANGING DROP, temperature 298K |
