1ZXZ

X-ray structure of peptide deformylase from Arabidopsis thaliana (AtPDF1A); crystals grown in PEG-5000 MME as precipitant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2005-01-30
Detector	MARRESEARCH 176mm
Wavelength(s)	0.979
Spacegroup name	P 21 21 21
Unit cell lengths	51.200, 73.800, 109.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.800
Rwork	0.236
R-free	0.29100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1y6h
RMSD bond length	0.007
RMSD bond angle	1.432
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.800
Rmerge	0.105
Number of reflections	10552
<I/σ(I)>	13.2
Completeness [%]	99.0

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	Crystals grown in PEG-5000 MME as precipitant, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K