6XHC

Structure of glycinyl 5'-O-adenosine phosphoramidate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2019-02-17
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	C 1 2 1
Unit cell lengths	100.756, 32.686, 72.723
Unit cell angles	90.00, 90.46, 90.00

Refinement procedure

Resolution	41.600 - 1.600
R-factor	0.1862
Rwork	0.184
R-free	0.23740
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	AFK1
RMSD bond length	0.009
RMSD bond angle	1.345
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.660
High resolution limit [Å]	1.600	3.450	1.600
Rmerge	0.055	0.032	0.775
Rmeas	0.060	0.035	0.858
Rpim	0.024	0.014	0.363
Total number of observations	184557
Number of reflections	31715	3309	3137
<I/σ(I)>	10.2
Completeness [%]	99.4	99.7	98.9
Redundancy	5.8	6	5.4
CC(1/2)		0.999	0.680

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	PROTEIN WAS CRYSTALLIZED FROM 25%, PEG 3350, 20 MM SODIUM CITRATE, PH 5.5, Glycinyl-O5'-adenosine phosphoramidate was soaked into the crystals using a stock solution of 100 mM, to achieve ~35 mM in the soaking solution