1K3U

CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-08-10
Detector	MAR scanner 345 mm plate
Spacegroup name	C 1 2 1
Unit cell lengths	182.409, 59.718, 67.177
Unit cell angles	90.00, 94.52, 90.00

Refinement procedure

Resolution	20.000 - 1.700
R-factor	0.1547
Rwork	0.153
R-free	0.18800 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qop
RMSD bond length	0.029
RMSD bond angle	2.293
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	CNS
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.000	1.800
High resolution limit [Å]	1.700	1.700
Rmerge	0.048 *	0.123 *
Total number of observations	236589 *
Number of reflections	77570
<I/σ(I)>	14.4	2.5
Completeness [%]	97.7	94.2
Redundancy	3.05

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	293	PEG 8000, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	sodium bicine	50 (mM)	pH7.8
3	1	drop	sodium-EDTA	10 (mM)
4	1	drop	dithioerythritol	1 (mM)
5	1	drop	pyridoxal phosphate	0.020 (mM)
6	1	reservoir	PEG8000	9-12 (%)
7	1	reservoir	spermine	1.5 (mM)
8	1	reservoir	EDTA	1 (mM)
9	1	reservoir	sodium bicine	50 (mM)	pH7.8