1HL2

Crystal structure of N-acetylneuraminate lyase from E. coli mutant L142R in complex with b-hydroxypyruvate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Collection date	2002-09-15
Spacegroup name	P 1 21 1
Unit cell lengths	83.740, 95.990, 89.650
Unit cell angles	90.00, 115.16, 90.00

Refinement procedure

Resolution	37.400 - 1.800
R-factor	0.183
Rwork	0.183
R-free	0.21000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fdy
RMSD bond length	0.009
RMSD bond angle	1.500
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.400	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.071	0.300
Total number of observations	412908 *
Number of reflections	117329
<I/σ(I)>	5.2	2.4
Completeness [%]	98.8	97.7
Redundancy	3.5	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.6 *	21 *	pH 4.60

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	BHP	20 (mM)
3	1	drop	Tris	20 (mM)	pH7.6
4	1	reservoir	sodium acetate	100 (mM)	pH4.6
5	1	reservoir	PEG4000	8 (%(w/v))