1HL8

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE

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	2001-03-03
Detector	ADSC CCD
Spacegroup name	H 3 2
Unit cell lengths	172.462, 172.462, 167.414
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	37.000 * - 2.400
R-factor	0.188
Rwork	0.185
R-free	0.22840 *
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	1.100 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.000 *	2.460
High resolution limit [Å]	2.400	2.400
Rmerge	0.069	0.416
Total number of observations	212598 *
Number of reflections	36833
<I/σ(I)>	8.9	1.8
Completeness [%]	99.3 *	99.3 *
Redundancy	5.7	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8	20 *	18 % PEG600, 5 % JEFFAMINE, M-600 100 MM TRIS-HCL PH 8.0, PROTEIN CONC. 5 MG/ML

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.0 (mg/ml)
2	1	reservoir	PEG6000	18 (%(w/v))
3	1	reservoir	Tris-HCl	100 (mM)	pH8.0
4	1	reservoir	Jeffamine M-600	5 (%)