3HZL
Tyr258Phe mutant of NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: open form at 1.55A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2008-06-27 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 88.390, 90.530, 85.970 |
| Unit cell angles | 90.00, 118.36, 90.00 |
Refinement procedure
| Resolution | 38.890 - 1.550 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.24400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2olo |
| RMSD bond length | 0.786 |
| RMSD bond angle | 5.400 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.590 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.065 | 0.401 |
| Number of reflections | 86058 | |
| <I/σ(I)> | 27 | 3 |
| Completeness [%] | 99.6 | 97.4 |
| Redundancy | 6.2 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 298 | 4 mL of the Tyr258Phe mutant protein (at 10 mg/mL) was mixed with 4 mL 20-30% 2-methyl-2,4-pentanediol (MPD) in 100 mM MES buffer (pH 5.7) and equilibrated against a reservoir of the latter solution, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |
