1AW2

TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS

Experimental procedure

Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1996-11
Detector	MAR scanner 300 mm plate
Spacegroup name	P 1 21 1
Unit cell lengths	89.660, 137.820, 89.540
Unit cell angles	90.00, 90.94, 90.00

Refinement procedure

Resolution	8.000 - 2.650
R-factor	0.2
Rwork	0.200
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	LIGANDED STRUCTURE (PDB ENTRY 1AFI)
RMSD bond length	0.015
RMSD bond angle	24.200 *
Data reduction software	DENZO
Data scaling software	CCP4
Phasing software	AMoRE
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.700
High resolution limit [Å]	2.650	2.650
Rmerge	0.101	0.298
Total number of observations	166818 *
Number of reflections	60048
<I/σ(I)>	11	6.7
Completeness [%]	95.7	95.8
Redundancy	3.1	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	4 *	100MM TRIETHANOLAMINE/HCL 100MM AMMONIUM SULFATE, 1MM DTT, EDTA, NAN3 1.26M SODIUM CITRATE PH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	triethanolamine-HCl	10 (mM)
3	1	reservoir		25 (mM)
4	1	reservoir	dithiothreitol	1 (mM)
5	1	reservoir	EDTA	1 (mM)
6	1	reservoir		1 (mM)
7	1	reservoir	2PG	20 (mM)