1I4J

CRYSTAL STRUCTURE OF L22 RIBOSOMAL PROTEIN MUTANT

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	2000-01-01
Detector	MARRESEARCH
Wavelength(s)	1.54179
Spacegroup name	P 1 21 1
Unit cell lengths	31.880, 86.590, 38.960
Unit cell angles	90.00, 104.47, 90.00

Refinement procedure

Resolution	23.170 - 1.800
R-factor	0.208
Rwork	0.209
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1BXE WITH REMOVED BETA-LOOP
RMSD bond length	0.007
RMSD bond angle	22.060 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.200 *	1.910
High resolution limit [Å]	1.800	1.800
Rmerge	0.074	0.331 *
Total number of observations	64827 *
Number of reflections	16162	1334 *
<I/σ(I)>	74.7	71.3
Completeness [%]	85.6	47.3
Redundancy	4. *	3. *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5 *	293 *	Davydova, N., (2001) Acta Crystallogr., Sect.D, 57, 1150. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	sodium acetate	50 (mM)	pH5.5
3	1	drop		200 (mM)
4	1	reservoir		1.9 (M)
5	1	reservoir	ethanol	3 (%)