8UAZ

Structure of Glutamyl-5'-O-adenosine phosphoramidate/RNase A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	LIQUID ANODE
Source details	BRUKER METALJET
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-01-17
Detector	Bruker PHOTON II
Wavelength(s)	1.3418
Spacegroup name	C 1 2 1
Unit cell lengths	101.255, 32.957, 73.987
Unit cell angles	90.00, 90.43, 90.00

Refinement procedure

Resolution	19.930 - 1.760
R-factor	0.21066
Rwork	0.209
R-free	0.24935
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.193
Data reduction software	PROTEUM PLUS
Data scaling software	PROTEUM PLUS
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.930	1.860
High resolution limit [Å]	1.760	1.760
Rmerge	0.095	0.701
Number of reflections	24382	3478
<I/σ(I)>	22.18	2.59
Completeness [%]	98.9	93.9
Redundancy	20	7.08

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	PROTEIN WAS CRYSTALLIZED FROM 25 percent PEG 3350, 20 MM SODIUM CITRATE, PH 5.5. Glutaminyl-5'-O-adenosine phosphoramidate soaking was achieved as follows. 1 uL of a stock solution of 100 mM ligand was added to 2uL of reservoir solution, to achieve a concentration of ~35 mM in the soaking solution. A few RNase A crystals were soaked for 110 - 130 minutes in the soaking solution.