1E1T

LYSYL-TRNA SYNTHETASE (LYSU) HEXAGONAL FORM COMPLEXED WITH THE LYSYL_ADENYLATE INTERMEDIATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1995-06-15
Detector	MARRESEARCH
Spacegroup name	P 61 2 2
Unit cell lengths	143.100, 143.100, 176.100
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.400
R-factor	0.186
Rwork	0.186
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e1o
RMSD bond length	0.007
RMSD bond angle	17.000 *
Data reduction software	DENZO
Data scaling software	CCP4
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.440
High resolution limit [Å]	2.400	2.400
Rmerge	0.086	0.204
Total number of observations	334798 *
Number of reflections	41908
<I/σ(I)>	10.5	4.1
Completeness [%]	98.2	94.1
Redundancy	8	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *		THE PROTEIN WAS CONCENTRATED TO 12 MG/ML IN THE PRESENCE OF 5MM LYSINE AND WAS CRYSTALLISED FROM 0.1 M PIPES PH 6.8, 0.5 M LICL, 20% PEG 4K, 17% GLYCEROL; THEN, A SMALL AMOUNT OF A SOLUTION CONTAINING ATP AND MGCL2 WAS ADDED TO THE DROP TO GET A FINAL CONCENTRATION OF ABOUT 5 MM.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	drop	HEPES	20 (mM)
3	1	drop	lysine	5 (mM)
4	1	drop	beta-mercaptoethanol	2 (mM)
5	1	reservoir	PEG2000	20 (%)
6	1	reservoir		0.5 (M)
7	1	reservoir	PIPES	0.1 (M)