2Z2P

Crystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with Quinupristin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	95
Detector technology	IMAGE PLATE
Collection date	2006-01-01
Detector	RIGAKU RAXIS IV++
Spacegroup name	P 21 21 21
Unit cell lengths	70.999, 93.700, 95.301
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.180 - 2.800
R-factor	0.268
Rwork	0.262
R-free	0.31800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2z2n
RMSD bond length	0.009
RMSD bond angle	1.512
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.990
High resolution limit [Å]	2.800	2.800
Number of reflections	14813
<I/σ(I)>	6	3.8
Completeness [%]	91.1	94.1
Redundancy	4.1	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5		100MM MES BUFFER (PH 6.5), 20%(W/V) PEG 10000, PROTEIN SOLUTION SUPPLEMENTED WITH 3MM MGCL2, 3MM DALFOPRISTIN, 1MM QUINUPRISTIN, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K