1FDZ

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION

Experimental procedure

Source type	ROTATING ANODE
Source details	MACSCIENCE M18X
Temperature [K]	108
Detector technology	IMAGE PLATE
Collection date	1995-12
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 32 2 1
Unit cell lengths	121.000, 121.000, 196.120
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.600
R-factor	0.2
Rwork	0.200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1FDZ (ENZYME-3-HYDROXYPYRUVATE COMPLEX)
RMSD bond length	0.012
RMSD bond angle	23.200 *
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]	15.000	2.640
High resolution limit [Å]	2.600	2.600
Rmerge	0.094	0.389
Total number of observations	203660 *
Number of reflections	49914
<I/σ(I)>	12.6	2.67
Completeness [%]	97.0	74 *
Redundancy	3.7	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	7.2 *	4 *	HANGING DROP VAPOR DIFFUSION. WELL: 53% SATURATED AMMONIUM SULFATE, 75 MILLIMOLAR SODIUM PHOSPHATE BUFFER (PH 6.9). DROP: EQUAL VOLUMES OF WELL AND PRE-REACTED ENZYME, SIALIC ACID AND BOROHYDRIDE MIX (SEE JRNL), vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	sodium phosphate	20 (mM)
2	1	1	azide	0.02 (%)