8OOW

Glutamine synthetase from Methermicoccus shengliensis at a resolution of 2.64 A

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06DA
Synchrotron site	SLS
Beamline	X06DA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-09-04
Detector	DECTRIS PILATUS 2M-F
Wavelength(s)	1.00004
Spacegroup name	P 1 21 1
Unit cell lengths	130.920, 195.646, 133.443
Unit cell angles	90.00, 94.71, 90.00

Refinement procedure

Resolution	62.960 - 2.640
R-factor	0.1931
Rwork	0.191
R-free	0.22520
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.350
Data reduction software	autoPROC
Data scaling software	STARANISO
Phasing software	PHASER
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	109.987	2.933
High resolution limit [Å]	2.636	2.636
Rmerge	0.076	0.870
Rmeas	0.084	0.989
Rpim	0.035	0.467
Number of reflections	123574	6180
<I/σ(I)>	15.5	1.6
Completeness [%]	90.3	78.7
Redundancy	5.7	4.4
CC(1/2)	0.999	0.600

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.6	293.15	The protein was crystallized fresh without any freezing step, and obtained through the sitting drop method on a 96-Well MRC 2-Drop Crystallization Plates in polystyrene (SWISSCI, United Kingdom) under anaerobic conditions (N2:H2, gas ratio of 97:3). Crystallization was performed at 9 mg/ml glutamine synthetase in 25 mM Tris/HCl pH 7.6, 10% glycerol, and 2 mM dithiothreitol. The reservoir contained 90 ul precipitant the following crystallization solution: 200 mM ammonium formate and 20 % (w/v) polyethylene glycol 3,350. 0.55 uL protein was mixed with 0.55 uL precipitant. Crystals were soaked in mother liquor with 25% v/v ethylene glycol before freezing in liquid nitrogen.