2DAA

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY D-CYCLOSERINE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	278
Detector technology	IMAGE PLATE
Collection date	1996-06-14
Detector	RIGAKU RAXIS II
Spacegroup name	P 21 21 21
Unit cell lengths	77.301, 91.018, 89.701
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.185 *
Rwork	0.205
R-free	0.23900 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1daa
RMSD bond length	0.007
RMSD bond angle	24.494 *
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	2.200
High resolution limit [Å]	2.000	2.000
Rmerge	0.055	0.293
Total number of observations	83705 *
Number of reflections	36340
<I/σ(I)>	15.9	3.5
Completeness [%]	97.9	99.1
Redundancy	2.47	2.35

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6 *		PROTEIN 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 22-26% PEG 4000, 0.2-0.3 M SODIUM ACETATE, 25 MM CYCLOSERINE 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	30 (mg/ml)
2	1	drop	potassium phosphate	100 (mM)
3	1	drop	PLP	0.05 (mM)
4	1	drop	beta-mercaptoethanol	0.01 (mM)
5	1	reservoir	D-cycloserine	25 (mM)
6	1	reservoir	PEG3350	26 (%)
7	1	reservoir	sodium acetate	200-300 (mM)
8	1	reservoir	Tris-Cl	100 (mM)