1GK3

Histidine Ammonia-Lyase (HAL) Mutant D145A from Pseudomonas putida

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUB200
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	I 2 2 2
Unit cell lengths	78.815, 117.105, 130.072
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	21.000 - 2.250
R-factor	0.221
R-free	0.28000
Structure solution method	OTHER
RMSD bond length	0.005
RMSD bond angle	0.016
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	SHELX

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	21.000
High resolution limit [Å]	2.250
Rmerge	0.126	0.290 *
Number of reflections	26022
<I/σ(I)>	2.4
Completeness [%]	91.0	95 *
Redundancy	2.3	2.2 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	3.85 *		Schwede, T.F., (1999) Protein Eng., 12, 151. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	sodium potassium phosphate	1.6 (M)
3	1	reservoir	HEPES	0.1 (M)
4	1	reservoir	EDTA	1.5 (mM)
5	1	reservoir	dioxane	3 (%)	pH3.85