4ZA1
Crystal Structure of NosA Involved in Nosiheptide Biosynthesis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-04-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9794 |
Spacegroup name | P 41 3 2 |
Unit cell lengths | 143.371, 143.371, 143.371 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
R-factor | 0.263 |
Rwork | 0.179 |
R-free | 0.21500 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 5.380 | 2.500 |
Rmerge | 0.092 | 0.041 | 0.464 |
Total number of observations | 1483177 | ||
Number of reflections | 18105 | ||
<I/σ(I)> | 12 | ||
Completeness [%] | 100.0 | 99.8 | 100 |
Redundancy | 81.9 | 76.2 | 81.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 291 | PEG 5100 |