1MGV

Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	CCD
Collection date	2001-09-26
Detector	MARRESEARCH
Wavelength(s)	1.12
Spacegroup name	C 1 2 1
Unit cell lengths	127.880, 55.899, 116.237
Unit cell angles	90.00, 110.06, 90.00

Refinement procedure

Resolution	20.080 - 2.100
R-factor	0.2031
Rwork	0.201
R-free	0.23300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	WT dimer
RMSD bond length	0.013 *
RMSD bond angle	1.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.210
High resolution limit [Å]	2.100	2.100
Rmerge	0.068 *	0.168 *
Total number of observations	177643 *
Number of reflections	43771 *
<I/σ(I)>	15.8	5.3
Completeness [%]	99.2	97.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.3 *	294	Kack, H., (1998) Acta Crystallogr., D54, 1397. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG4000	21 (%)	pH7.3
3	1	reservoir	2-propanol	12 (%)