3RSK

STRUCTURE OF THE K7A/R10A/K66A VARIANT OF RIBONUCLEASE A

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	273
Detector technology	AREA DETECTOR
Collection date	1997-09-11
Detector	SIEMENS
Spacegroup name	P 32 2 1
Unit cell lengths	68.150, 68.150, 65.510
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rph
RMSD bond length	0.010
RMSD bond angle	17.868 *
Data reduction software	XCALIBRE
Data scaling software	XDS
Phasing software	AMoRE
Refinement software	TNT (5E)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.029 *	0.171 *
Total number of observations	33804 *
Number of reflections	14929 *
<I/σ(I)>	20
Completeness [%]	91.0	84
Redundancy	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	20 *	CRYSTALS WERE PREPARED USING THE HANGING DROP METHOD. LYOPHILIZED K7A/R10A/K66A RNASE A WAS DISSOLVED IN UNBUFFERED WATER TO A CONCENTRATION OF 60MG/ML. DROPS CONSISTING OF PROTEIN SOLUTION (1.5UL), WATER (1.5UL), AND RESERVOIR SOLUTION (3.0UL) WERE SUSPENDED OVER 0.5 ML OF RESERVOIR SOLUTION [0.1M SODIUM ACETATE BUFFER, PH 4.5, CONTAINING 36% PEG 4000., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	60 (mg/ml)
2	1	drop	water		0.0015mM
3	1	reservoir	sodium acetate	0.1 (M)
4	1	reservoir	PEG4000	36 (%(w/v))