1GYJ

The Crystal Structure of YdcE, a 4-Oxalocrotonate Tautomerase Homologue from Escherichia coli, Confirms the Structural Basis for Oligomer Diversity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2001-12-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	37.250, 63.810, 71.340
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.225
Rwork	0.225
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	UNPUBLISHED 1.35 ANG. RES. YDCE STRUCTURE DETERMINED BY MIR
RMSD bond length	0.008 *
RMSD bond angle	1.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.092	0.435 *
Total number of observations	169053 *
Number of reflections	10344
<I/σ(I)>	11.5	3
Completeness [%]	99.7	99.1
Redundancy	16	10

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5 *	4 *	PROTEIN BUFFERED IN 50MM SODIUM PHOSPHATE, PH 7.3 PRECIPITANT: 40% SODIUM CITRATE PH 8.5 ITTING DROP: MIX 5UL PROT. WITH 5UL 40% SODIUM CITRATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	sodium citrate	40 (%(w/v))	pH8.5