1NIO

Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	290
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	89.902, 59.823, 55.184
Unit cell angles	90.00, 120.81, 90.00

Refinement procedure

Resolution	29.210 - 2.000
R-factor	0.162
Rwork	0.162
R-free	0.20300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	23.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.111	0.422 *
Total number of observations	60539 *
Number of reflections	17034 *
Completeness [%]	99.6	98.9 *
Redundancy	3.54 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-HCl	0.05 (M)	pH7.5
2	1	reservoir	ammonium sulfate	40 (%(w/v))
3	1	drop	protein	40 (mg/ml)
4	1	drop		0.15 (M)
5	1	drop		0.1 (%(w/v))