3IUK
Crystal structure of putative bacterial protein of unknown function (DUF885, PF05960.1, ) from Arthrobacter aurescens TC1, reveals fold similar to that of M32 carboxypeptidases
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9794,0.9795 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.614, 85.394, 115.489 |
| Unit cell angles | 90.00, 90.78, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.850 |
| R-factor | 0.16633 |
| Rwork | 0.163 |
| R-free | 0.21994 |
| Structure solution method | MAD |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.623 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.091 | 0.530 |
| Number of reflections | 98606 | |
| <I/σ(I)> | 16 | 2 |
| Completeness [%] | 99.7 | 99.5 |
| Redundancy | 3.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.2 MgCl, 25% Peg3350, 0.1 M Hepes , pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
