5DAA

E177K MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	278
Detector technology	IMAGE PLATE
Collection date	1998-01-12
Detector	RIGAKU RAXIS II
Spacegroup name	P 21 21 21
Unit cell lengths	77.850, 91.870, 89.380
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.900
Rwork	0.195
R-free	0.24500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daa
RMSD bond length	0.007
RMSD bond angle	23.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.200
High resolution limit [Å]	2.900	2.900
Rmerge	0.144	0.337
Total number of observations	39415 *
Number of reflections	13649 *
<I/σ(I)>	9.9	4.9
Completeness [%]	93.1	94.1
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.3 *		PDA INACTIVATED PROTEIN WAS CONCENTRATED TO 30 MG/ML IN 0.1 M 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 27% PEG 4000, 0.4 M SODIUM ACETATE, AND 0.1 M TRIS-CHLORIDE PH 8.5., vapor diffusion - hanging drop

Crystallization Reagents

ID	crystal ID	solution ID	reagent name	concentration	details
1	1	1	K3PO4
2	1	1	BETA-MERCAPTOETHANOL
3	1	1	PEG 4000
4	1	1	TRIS-CHLORIDE
5	1	1	sodium acetate

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	0.05 (M)
6	1	reservoir	PEG3350	26 (%)
7	1	reservoir	sodium acetate	0.3 (M)
8	1	reservoir	Tris-HCl	0.1 (M)