8UB2

Structure of Adenosine monophosphate/RNase A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	LIQUID ANODE
Source details	BRUKER METALJET
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-09-05
Detector	Bruker PHOTON II
Wavelength(s)	1.3418
Spacegroup name	C 1 2 1
Unit cell lengths	101.054, 32.514, 72.935
Unit cell angles	90.00, 90.81, 90.00

Refinement procedure

Resolution	20.640 - 1.600
R-factor	0.23803
Rwork	0.237
R-free	0.26238
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.489
Data reduction software	APEX
Data scaling software	APEX
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.640	1.700
High resolution limit [Å]	1.600	1.600
Rmerge	0.084	0.542
Number of reflections	29170	4826
<I/σ(I)>	5.47	1.35
Completeness [%]	91.9	92.6
Redundancy	2.25	1.35

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. 5'-O-adenosine monophoshate 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 ~33 mM in the soaking solution. A few RNase A crystals were soaked for 160 - 180 minutes in the soaking solution