4HSN
Crystal structure of 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 | 73.462, 137.279, 76.360 |
Unit cell angles | 90.00, 96.42, 90.00 |
Refinement procedure
Resolution | 19.790 - 2.000 |
R-factor | 0.1774 |
Rwork | 0.175 |
R-free | 0.20850 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1of8 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.781 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.790 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 100515 | |
Completeness [%] | 99.3 | 100 |
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 |