1AX4

TRYPTOPHANASE FROM PROTEUS VULGARIS

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1994-01
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	114.990, 118.230, 153.680
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.000 - 2.100
R-factor	0.187 *
Rwork	0.187
R-free	0.22749
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	TYROSINE PHENOL LYASE PDB ENTRY 1TPL
RMSD bond length	0.012 *
RMSD bond angle	0.030 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.000	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.098	0.273
Total number of observations	397510 *
Number of reflections	117863 *
<I/σ(I)>	11	3.2
Completeness [%]	97.6	97.3
Redundancy	3.33	2.49

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.8		27 % PEG 4000, 0.1 M POTASSIUM PHOSPHATE BUFFER PH 7.8, 0.25 MM PYRIDOXAL 5'-PHOSPHATE, 5MM DTT, 0.1 M CSCL.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PLP	0.25 (mM)
2	1	reservoir	dithiothreitol	5 (mM)
3	1	reservoir		0.1 (M)
4	1	reservoir	potassium phosphate	0.1 (M)
5	1	reservoir	PEG4000	27 (%)