1URX

Crystallographic structure of beta-agarase A in complex with oligoagarose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	193
Collection date	2003-03-15
Spacegroup name	P 32 2 1
Unit cell lengths	51.380, 51.380, 205.360
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	37.200 - 1.700
R-factor	0.15642
Rwork	0.155
R-free	0.18200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1o4y
RMSD bond length	0.015 *
RMSD bond angle	1.762 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.200	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.042	0.110
Total number of observations	148960 *
Number of reflections	34045
<I/σ(I)>	12.1	6.8
Completeness [%]	95.3	98.4
Redundancy	4.4	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	20.5 *	30 % PEG 4000 200 MM AMMONIUM ACETATE, 100 MM SODIUM ACETATE PH 4.6

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.5 (mg/ml)
2	1	drop	Tris	50 (mM)	pH7.5
3	1	drop		25 (mM)
4	1	drop	agaro-octaose	4 (mM)
5	1	reservoir	PEG4000	30 (%)
6	1	reservoir	ammonium acetate	200 (mM)
7	1	reservoir	sodium acetate	100 (mM)	pH4.6