1UC9

Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	100
Detector technology	CCD
Collection date	2002-07-04
Detector	MARRESEARCH
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	126.591, 52.145, 105.105
Unit cell angles	90.00, 123.24, 90.00

Refinement procedure

Resolution	49.800 - 2.380
Rwork	0.243
R-free	0.28000 *
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	23.400 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.470
High resolution limit [Å]	2.380	2.380
Rmerge	0.036	0.234
Number of reflections	22847
<I/σ(I)>	21.9	5.5
Completeness [%]	98.1	94.4
Redundancy	4.3	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	293	Vassylyeva, M.N., (2003) Acta Crystallogr., D59, 1651. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG4000	5 (%)
3	1	reservoir	sodium acetate	17 (mM)	pH4.6
4	1	reservoir	ammonium acetate	0.35 (mM)