1O4Z

THE THREE-DIMENSIONAL STRUCTURE OF BETA-AGARASE B FROM ZOBELLIA GALACTANIVORANS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2002-12-01
Detector	ADSC QUANTUM 4
Spacegroup name	P 1 21 1
Unit cell lengths	72.448, 105.350, 97.369
Unit cell angles	90.00, 94.13, 90.00

Refinement procedure

Resolution	24.800 * - 2.300
R-factor	0.16862
Rwork	0.166
R-free	0.22400 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	BETA-AGARASE A
RMSD bond length	0.031 *
RMSD bond angle	2.400 *
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.800 *	2.420
High resolution limit [Å]	2.300	2.300
Rmerge	0.106 *	0.339 *
Total number of observations	428617 *
Number of reflections	64783 *
<I/σ(I)>	5.4	1.6
Completeness [%]	99.9	99.9 *
Redundancy	3.5	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	20.5 *	58% methyl-pentane-diol 20 mM calcium chloride 100 mM Hepes , pH 7.5, VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.5 (mg/ml)
2	1	drop	Tris	50 (%(w/v))	pH7.5
3	1	drop		25 (mM)
4	1	reservoir	MPD	58 (%)
5	1	reservoir		20 (mM)
6	1	reservoir	HEPES	100 (mM)	pH7.5