5O4N

Apo HcgC from Methanococcus maripaludis soaked with SAH and pyridinol

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-02-17
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	1.00001
Spacegroup name	P 1 21 1
Unit cell lengths	72.556, 80.997, 97.808
Unit cell angles	90.00, 108.24, 90.00

Refinement procedure

Resolution	30.010 - 2.050
R-factor	0.1988
Rwork	0.197
R-free	0.23570
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5o4j
RMSD bond length	0.010
RMSD bond angle	1.150
Data reduction software	XDS
Data scaling software	SCALA (3.3.22)
Phasing software	MOLREP (11.4.06)
Refinement software	BUSTER (2.10.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.550	2.160
High resolution limit [Å]	2.050	2.050
Rmerge	0.103	0.717
Rpim	0.072	0.498
Number of reflections	65248	9601
<I/σ(I)>	6.2	1.4
Completeness [%]	96.7	98
Redundancy	2.9	2.9
CC(1/2)	0.993	0.600

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	281	The drop consists of 1 ul of enzyme solution containing 5 mg/ml HcgC mixed with 1 ul of the reservoir solution : 100 mM HEPES/NaOH pH 7.5, 0.1 M NaCl, and 30% MPD (2-Methyl-2,4-pentanediol). The soaking was performed overnight in the same crystallization buffer containing 2 mM SAH and 3 mM pyridinol (dissolved in 100% DMSO).