1H7M

Ribosomal Protein L30e from Thermococcus celer

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-07-17
Detector	MARRESEARCH
Spacegroup name	P 61
Unit cell lengths	48.320, 48.320, 86.420
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	24.200 * - 1.960
R-factor	0.17
Rwork	0.165
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	UNPUBLISHED NMR STRUCTURE OF THE SAME L30E PROTEIN
RMSD bond length	0.028 *
RMSD bond angle	2.220 *
Data reduction software	iMOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.200	2.070
High resolution limit [Å]	1.960	1.960
Rmerge	0.082	0.343
Number of reflections	8226
<I/σ(I)>	7.6	2.1
Completeness [%]	99.9	99.9
Redundancy	7.5	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.6	290 *	Wong, K.B., (2001) Acta Crystallogr.,Sect.D, D57, 865. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	24 (mg/ml)
2	1	reservoir	potassium phosphate	50 (mM)
3	1	reservoir	PEG8000	20 (%(w/v))