1MRL

Crystal structure of streptogramin A acetyltransferase with dalfopristin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	CCD
Collection date	2002-03-11
Detector	MARRESEARCH
Wavelength(s)	0.8700
Spacegroup name	P 21 21 21
Unit cell lengths	82.914, 90.905, 104.529
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.800
R-factor	0.2723
Rwork	0.271
R-free	0.30300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mr7
RMSD bond length	0.003
RMSD bond angle	1.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.870
High resolution limit [Å]	2.800	2.800
Rmerge	0.082	0.358
Total number of observations	222509 *
Number of reflections	20118
<I/σ(I)>	15.5	3.6
Completeness [%]	99.7 *	99.2 *
Redundancy	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		290	0.2M Sodium Fluoride, 20% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	0.25 (mM)
2	1	drop	dalfopristin	1.5 (mM)
3	1	reservoir	sodium fluoride	0.2 (M)
4	1	reservoir	PEG3350	20 (%(w/v))