4HSO
Crystal structure of S213G variant DAH7PS from Neisseria meningitidis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9537 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.523, 136.995, 76.212 |
Unit cell angles | 90.00, 96.63, 90.00 |
Refinement procedure
Resolution | 19.530 - 2.100 |
R-factor | 0.2059 |
Rwork | 0.204 |
R-free | 0.24240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hsn |
RMSD bond length | 0.015 |
RMSD bond angle | 1.610 |
Data scaling software | SCALA (3.3.20) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 19.571 | 19.571 | 2.210 |
High resolution limit [Å] | 2.100 | 6.640 | 2.100 |
Rmerge | 0.017 | 0.393 | |
Total number of observations | 9650 | 47490 | |
Number of reflections | 86154 | ||
<I/σ(I)> | 17.9 | 35 | 1.9 |
Completeness [%] | 98.8 | 94.9 | 99.7 |
Redundancy | 3.7 | 3.6 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293.15 | A protein solution [11 mg/mL in 10 mM BTP buffer (pH 7.3)] was mixed 1:1 (v/v) with a reservoir solution containing 0.2 M trimethylamine N-oxide, 0.1 M Tris (pH 8.5), 15% 20% (w/v) PEG 2000 mme, 0.4 mM MnSO4. The drop sizes were 2 uL, and the volume of the reservoir solution was 500 uL, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K |