1G2A

THE CRYSTAL STRUCTURE OF E.COLI PEPTIDE DEFORMYLASE COMPLEXED WITH ACTINONIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1999-04-28
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	138.700, 63.100, 85.600
Unit cell angles	90.00, 121.40, 90.00

Refinement procedure

Resolution	14.000 - 1.750
R-factor	0.191
Rwork	0.190
R-free	0.25000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	2.437 *
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.000	1.790
High resolution limit [Å]	1.750	1.750
Rmerge	0.044	0.191
Number of reflections	54729	3634 *
<I/σ(I)>	13.6
Completeness [%]	85.9 *	86.8
Redundancy	1.95	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	290	10mg/ml PDF, 20mM actinonin, 50mM HEPES, pH 7.5 + 25-32% PEG 4000, 0.1M sodium citrate, pH 5.6, 0.2M ammonium acetate, VAPOR DIFFUSION, HANGING DROP at 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	inhibitor	20 (mM)
3	1	drop	HEPES	50 (mM)
4	1	reservoir	PEG4000	25-32 (%)
5	1	reservoir	sodium citrate	0.1 (M)
6	1	reservoir	ammonium sulfate	0.2 (M)