2BV6

Crystal structure of MgrA, a global regulator and major virulence determinant in Staphylococcus aureus

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-ID-B
Synchrotron site	APS
Beamline	14-ID-B
Temperature [K]	77
Detector technology	CCD
Collection date	2005-04-03
Spacegroup name	P 61 2 2
Unit cell lengths	119.800, 119.800, 62.300
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	24.390 - 2.800
R-factor	0.25
Rwork	0.250
R-free	0.29200
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	1.400
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.500	2.980
High resolution limit [Å]	2.800	2.800
Rmerge	0.070	0.950
Number of reflections	8544
Completeness [%]	99.0	98
Redundancy	19.3	10

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.6		PROTEIN WAS CRYSTALLIZED FROM 1.6 M AMMONIUM SULFATE, 0.1M MES, PH 6.0, XTALS WERE RINSED IN CRYOPROTECTANT SOLUTIONS CONSISTING OF RESERVOIR BUFFER WITH AN ADDED 10%, 20% AND 25% GLYCEROL RESPECTIVELY. SELENOMETHIONINE (SEMET)-CONTAINING PROTEIN WAS CRYSTALLIZED UNDER THE SAME CONDITION.