1LMH

Crystal Structure of S. aureus peptide deformylase

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	1998-07-12
Detector	BRUKER
Wavelength(s)	1.03321, 0.97939, 0.97928
Spacegroup name	C 2 2 21
Unit cell lengths	94.131, 121.873, 47.579
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 * - 1.900
R-factor	0.18 *
Rwork	0.180
R-free	0.21200
Structure solution method	MAD
RMSD bond length	0.004
RMSD bond angle	22.900 *
Data reduction software	SAINT
Data scaling software	SAINT
Phasing software	MLPHARE
Refinement software	CNX (2000.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	1.968
High resolution limit [Å]	1.900	1.890 *
Rmerge	0.042 *	0.107 *
Number of reflections	21519 *
<I/σ(I)>	7.97
Completeness [%]	97.5
Redundancy	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8.5	293	used seeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	17-27 (%)
2	1	reservoir		200 (mM)
3	1	reservoir	Tris-HCl	100 (mM)	pH8.5