1BXY

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	298
Spacegroup name	P 32 2 1
Unit cell lengths	63.500, 63.500, 77.800
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 1.900
R-factor	0.203
Rwork	0.203
R-free	0.25300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.019
RMSD bond angle	3.079
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	80.000
High resolution limit [Å]	1.850 *
Rmerge	0.083 *	0.319 *
Total number of observations	150778 *
Number of reflections	35601 *
Completeness [%]	82.9 *	92.7 *
Redundancy	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		pH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15-20 (mg/ml)
2	1	drop	ammonium sulfate	0.8 (M)
3	1	drop	Tris-HCl	75 (mM)
4	1	reservoir	ammonium sulfate	2.5 (M)