8OOL

Glutamine synthetase from Methanothermococcus thermolithotrophicus with TbXo4 at a resolution of 1.65 A

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-10-01
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97625
Spacegroup name	C 2 2 21
Unit cell lengths	131.434, 228.448, 204.803
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.780 - 1.650
R-factor	0.1641
Rwork	0.163
R-free	0.18500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.485
Data reduction software	XDS
Data scaling software	SCALA (3.3.22)
Phasing software	MOLREP
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.780	1.740
High resolution limit [Å]	1.650	1.650
Rmerge	0.063	0.918
Rmeas	0.074	1.081
Rpim	0.039	0.566
Number of reflections	361584	51999
<I/σ(I)>	11.9	1.6
Completeness [%]	98.9	97.9
Redundancy	6.9	6.9
CC(1/2)	0.999	0.782

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Crystallization was performed in an anoxic tent (with a gas phase of 95% N2/5% H2) on a 96-well two-drop MRC crystallization plate in polystyrene (Molecular Dimensions, Suffolk, UK). The sitting drops contained a mix of 0.7 ml of the glutamine synthetase at 15 mg/ml with 10 mM TbXo4 and 0.7 ml of precipitant solution (35 % Pentaerythritol ethoxylate (15/4 EO/OH), 200 mM Ammonium sulphate, 100 mM HEPES pH 7.5).