6NE6
Crystal Structure of heterotrimeric G-protein alpha subunit Galpha7 from Naegleria fowleri
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-04-05 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.690, 68.310, 79.570 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.256 - 1.700 |
R-factor | 0.163 |
Rwork | 0.161 |
R-free | 0.19470 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5do9 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MoRDa |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.256 | 48.256 | 1.740 |
High resolution limit [Å] | 1.700 | 7.600 | 1.700 |
Rmerge | 0.046 | 0.022 | 0.512 |
Rmeas | 0.050 | 0.025 | 0.572 |
Total number of observations | 222267 | ||
Number of reflections | 37029 | 458 | 2695 |
<I/σ(I)> | 23.09 | 58.88 | 2.99 |
Completeness [%] | 99.8 | 96.2 | 99.8 |
Redundancy | 6.003 | 5.238 | 4.996 |
CC(1/2) | 0.999 | 0.999 | 0.858 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | NafoA.01088.e.B1 and NafoA.19531.b.B2 were co-purified (PW38434) to 20.24 mg/ml in a buffer containing 25 mM HEPES pH 7.5, 500 mM NaCl, 5% Glycerol , 2 mM DTT, 0.025% Azide, 10mM MgCl2, 10mM NaF, 30uM AlCl3, 5uM GDP, was mixed 1:1 with Wiz3/4(c8): 16% (w/v) PEG-800, 40 mM potassium phosphate monobasic, 20% (v/v) glycerol, cryoprotected with 20% ethylene glycol. Tray 299259c8, puck: rhn8-4 |