8A8G

ATP sulfurylase from Methanothermococcus thermolithotrophicus - orthorhombic form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 1
Synchrotron site	SOLEIL
Beamline	PROXIMA 1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-02-06
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.00000
Spacegroup name	I 2 2 2
Unit cell lengths	55.705, 154.457, 157.575
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.730 - 1.970
R-factor	0.19
Rwork	0.189
R-free	0.21790
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1v47
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHENIX
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	78.790	2.220
High resolution limit [Å]	1.970	1.970
Rmerge	0.151	1.740
Rmeas	0.157	1.806
Rpim	0.042	0.483
Number of reflections	28197	1410
<I/σ(I)>	12.7	1.6
Completeness [%]	93.2	62.3
Redundancy	13.7	13.9
CC(1/2)	0.998	0.641

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	Purified ATPS sulfurylase from Methanothermococcus thermolithotrophicus was concentrated to 14 mg.ml-1 in 25 mM Tris/HCl pH 7.6, 10% v/v glycerol, 2 mM dithiothreitol, and 150 mM NaCl. Crystals were obtained by mixing 0.7 ul of the sample with 0.7 ul of 35 % w/v Pentaerythritol ethoxylate (15/4 EO/OH), and 100 mM 2-(N-morpholino)ethanesulfonic acid (MES) pH 6.5 in a 96-Well MRC 2-drop crystallization plates in polystyrene (SWISSCI) containing 90 ul of crystallization solution in the reservoir.