3DAA

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-06-14
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	77.100, 78.300, 88.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.900
R-factor	0.195
Rwork	0.195
R-free	0.24500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daa
RMSD bond length	0.008
RMSD bond angle	23.862 *
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	1.850
High resolution limit [Å]	1.800	1.800
Rmerge	0.062	0.293
Total number of observations	57553 *
Number of reflections	43763
<I/σ(I)>	15.9	3.5
Completeness [%]	87.1	76.1
Redundancy	2.47	2.35

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6 *		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, 0.3 M SODIUM ACETATE, 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	Tris-Cl	100 (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	13-14 (%)
6	1	drop	sodium acetate	150 (mM)
7	1	drop	Tris-Cl	50 (mM)
8	1	reservoir	PEG4000	26-28 (%)
9	1	reservoir	sodium acetate	300 (mM)