1E71

MYROSINASE FROM SINAPIS ALBA with bound ascorbate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	1997-10-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	135.300, 137.200, 80.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.500
R-factor	0.123 *
Rwork	0.127
R-free	0.15200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e4m
RMSD bond length	0.019
RMSD bond angle	0.034
Data reduction software	MOSFLM
Data scaling software	Agrovata
Phasing software	X-PLOR
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.800	1.580
High resolution limit [Å]	1.500	1.500
Rmerge	0.065	0.294
Number of reflections	110239
<I/σ(I)>	5.8	2
Completeness [%]	95.6	91.5
Redundancy	3.7	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5 *		Burmeister, W.P., (1997) Structure (London), 5, 663. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	myrosinase	12 (mg/ml)
2	1	drop	HEPES	30 (mM)
3	1	drop		0.05 (%)
4	1	reservoir	ammonium sulfate	66 (%sat)
5	1	reservoir	Tris-HCl	100 (mM)