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 |