1LME

Crystal Structure of Peptide Deformylase from Thermotoga maritima

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2002-01-08
Detector	ADSC QUANTUM 4
Spacegroup name	P 32 2 1
Unit cell lengths	65.048, 65.048, 151.371
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 2.200
R-factor	0.198
Rwork	0.198
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bs4
RMSD bond length	0.010
RMSD bond angle	24.400 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	2.340
High resolution limit [Å]	2.200	2.200
Rmerge	0.075 *	0.327 *
Number of reflections	19503
<I/σ(I)>	10.8
Completeness [%]	99.6 *	98.8 *
Redundancy	7.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.9	20 *	PEG 3350, potassium nitrate, pH 6.9, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3350	20 (%(w/v))
2	1	reservoir	potassium nitrate	0.2 (M)	pH6.9