4DAA

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE IN PYRIDOXAL-5'-PHOSPHATE (PLP) FORM

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	278
Detector technology	IMAGE PLATE
Collection date	1996-08
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	141.100, 68.900, 87.400
Unit cell angles	90.00, 119.50, 90.00

Refinement procedure

Resolution	30.000 - 2.400
R-factor	0.181
Rwork	0.181
R-free	0.24700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daa
RMSD bond length	0.007
RMSD bond angle	23.965 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.500
High resolution limit [Å]	2.250	2.250
Rmerge	0.149 *	0.293
Total number of observations	92975 *
Number of reflections	31959
<I/σ(I)>	17.1	4.4
Completeness [%]	91.9	69.5
Redundancy	2.91	2.35

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6 *		PROTEIN WAS CONCENTRATED TO 30 MG/ML IN 100 MM POTASSIUM PHOSPHATE BUFFER PH 7.6 CONTAINING 50 UM PLP AND 0.001 BETA-MERCAPTOETHANOL. CRYSTALS WERE THEN GROWN BY THE HANGING DROP METHOD IN 25% PEG 4000, 200 MM AMMONIUM SULFATE, 100 MM SODIUM ACETATE, 1 MM ALPHA-KETOGLUTARATE, AND 0.1 M TRIS-CHLORIDE PH 8.5., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
10	1	reservoir	ammonium sulfate	200 (mM)
11	1	reservoir	sodium acetate	100 (mM)
12	1	reservoir	alpha-ketoglutarate	1 (mM)
2	1	drop	potassium phosphate	50 (mM)
3	1	drop	PLP	0.025 (mM)
4	1	drop	beta-mercaptoethanol	0.005 (mM)
5	1	drop	PEG4000	12.5 (%)
6	1	drop	ammonium sulfate	100 (mM)
7	1	drop	sodium acetate	50 (mM)
8	1	drop	alpha-ketoglutarate	0.5 (mM)
9	1	reservoir	PEG4000	25 (%)