2PTH

PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI

Experimental procedure

Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	273
Detector technology	IMAGE PLATE
Collection date	1996-02
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	47.240, 63.590, 62.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.200
R-factor	0.196
Rwork	0.196
R-free	0.21500
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENTS
RMSD bond length	0.008
RMSD bond angle	22.500 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.000	1.230
High resolution limit [Å]	1.200	1.200
Rmerge	0.046 *
Number of reflections	55575
<I/σ(I)>	8.3	4.6
Completeness [%]	93.9	85.3
Redundancy	4.2	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	6 *	Schmitt, E., (1997) Proteins.Struct.Funct.Genet., 28, 135. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	10-12 (%)
2	1	reservoir	isopropanol	12 (%)
3	1	reservoir	Tris-HCl	0.1 (M)
4	1	drop	protein	2 (mg/ml)