1G2W

E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1999-04-29
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	77.187, 90.522, 89.097
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.000 * - 2.000
R-factor	0.188
Rwork	0.188
R-free	0.22700
RMSD bond length	0.006
RMSD bond angle	22.590 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.000	2.140
High resolution limit [Å]	1.800	1.800 *
Rmerge	0.123	0.244 *
Total number of observations	303396 *
Number of reflections	96070
<I/σ(I)>	10
Completeness [%]	85.4 *	97.5 *
Redundancy	3.2	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.3 *	277	resevoir: Tris-HCl, pH 8.5, 22-26% PEG 4K, 0.2-0.4M NaOAc, 1mM alpha-ketoglutarate, enzyme buffer: 50mM KPO4, pH 7.2, 200mM KCl, 1mM DTT, 10uM PLP , VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	30 (mg/ml)
2	1	drop	potassium phosphate	50 (mM)
3	1	drop		0.13 (M)
4	1	drop	EDTA	0.2 (mM)
5	1	drop	PLP	50 (mM)
6	1	drop	beta-mercaptoethanol	0.01 (%)
7	1	reservoir	PEG3350	26 (%)
8	1	reservoir	sodium acetate	0.3 (M)
9	1	reservoir	Tris-HCl	0.1 (M)