1S07

Crystal Structure of the R253A Mutant of 7,8-Diaminopelargonic Acid Synthase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-08-22
Detector	MARRESEARCH
Wavelength(s)	0.85
Spacegroup name	P 1 21 1
Unit cell lengths	58.080, 56.527, 120.993
Unit cell angles	90.00, 96.32, 90.00

Refinement procedure

Resolution	20.000 - 2.400 *
R-factor	0.18968
Rwork	0.188
R-free	0.22500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	WT dimer
RMSD bond length	0.016
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]	20.000	2.480
High resolution limit [Å]	2.400 *	2.420
Rmerge	0.077 *	0.248 *
Total number of observations	86216 *
Number of reflections	26936
<I/σ(I)>	14.8	24.8
Completeness [%]	90.6	55.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	20 *	PEG4000, MPD, HEPES, isopropanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	26-28 (%)
2	1	reservoir	MPD	9-12 (%)
3	1	reservoir	HEPES	100 (mM)	pH7.5
4	1	drop	protein	10 (mg/ml)