1FDY

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE

Experimental procedure

Source type	ROTATING ANODE
Source details	MACSCIENCE M18X
Temperature [K]	108
Detector technology	IMAGE PLATE
Collection date	1995-09
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 32 2 1
Unit cell lengths	121.000, 121.000, 196.820
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.450
R-factor	0.219
Rwork	0.219
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nal
RMSD bond length	0.012
RMSD bond angle	23.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.490
High resolution limit [Å]	2.450	2.440
Rmerge	0.041	0.245
Total number of observations	148263 *
Number of reflections	60890
<I/σ(I)>	13.6	4.15
Completeness [%]	92.5	78 *
Redundancy	2.43	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.9	37 *	HANGING DROP VAPOR DIFFUSION. WELL: 53% SATURATED AMMONIUM SULFATE, 75 MILLIMOLAR SODIUM PHOSPHATE BUFFER (PH 6.9). DROP: EQUAL VOLUMES OF WELL SOLUTION AND PRE-REACTED ENZYME/HYDROXYPYRUVATE COMPLEX (SEE JRNL REFERENCE), vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium salfate	53 (%(v/v)sat)
2	1	reservoir	sodium phosphate	75 (mM)
3	1	drop	protein	6.9 (mg/ml)