1OEP

Structure of Trypanosoma brucei enolase reveals the inhibitory divalent metal site

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU ULTRAX 18
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-10-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	74.018, 110.536, 109.098
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.820 - 2.300
R-factor	0.21
Rwork	0.210
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1one
RMSD bond length	0.007
RMSD bond angle	23.100 *
Data reduction software	AUTOMAR
Data scaling software	AUTOMAR
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.800 *	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.065	0.468
Number of reflections	20116
<I/σ(I)>	14.2	1.9
Completeness [%]	97.2 *	93.4
Redundancy	4.7	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5	18 *	Hannaert, V., (2003) Eur.J.Biochem., 270, 3205. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)