1E2A

ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1995-10-01
Detector	MARRESEARCH
Spacegroup name	P 41 21 2
Unit cell lengths	90.900, 90.900, 82.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.19
Rwork	0.190
R-free	0.24000
Structure solution method	SINGLE ISOMORPHOUS REPLACEMENT AND ANOMALOUS SCATTERING (SIRAS)
RMSD bond length	0.005
RMSD bond angle	16.940 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.400
High resolution limit [Å]	2.300	2.300
Rmerge	0.086 *	0.363 *
Number of reflections	16632
<I/σ(I)>	18.3	4.9
Completeness [%]	97.7	98.9
Redundancy	6.1	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.4	25 *	CRYSTALS WERE OBTAINED BY THE SITTING-DROP VAPOR-DIFFUSION TECHNIQUE AT ROOM TEMPERATURE USING A SMALL INCREASE IN THE PHOSPHATE BUFFER. THE PROTEIN SOLUTION WAS MIXED WITH 0.15M NA/K PHOSPHATE BUFFER, PH 6.4. THE LARGEST CRYSTALS APPEARED IN CIRCA A WEEK., vapor diffusion - sitting drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	sodium potassium phosphate	150 (mM)
3	1	reservoir	sodium potassium phosphate	400 (mM)