1O9N

Crystal structure of the K62A mutant of Malonamidase E2 from Bradyrhizobium japonicum

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	RIGAKU IMAGE PLATE
Spacegroup name	P 21 21 2
Unit cell lengths	103.246, 94.498, 75.430
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.173
Rwork	0.173
R-free	0.23700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1GR8
RMSD bond length	0.003 *
RMSD bond angle	1.034 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.069 *	0.217 *
Total number of observations	384083 *
Number of reflections	50620
<I/σ(I)>	12.4	3.2
Completeness [%]	89.0	76.1
Redundancy	3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7		20% POLYETHYLENE GLYCOL 1000, 100 MM TRIS, PH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG1000	20 (%)
3	1	reservoir	Tris-HCl	0.1 (M)	pH7.0