1FA5

CRYSTAL STRUCTURE OF THE ZN(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	200
Detector technology	IMAGE PLATE
Collection date	1999-03-18
Detector	RIGAKU RAXIS II
Spacegroup name	P 1 21 1
Unit cell lengths	46.240, 57.170, 46.990
Unit cell angles	90.00, 95.36, 90.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.186 *
Rwork	0.186
R-free	0.26000
RMSD bond length	0.007
RMSD bond angle	1.603
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.046	0.052
Total number of observations	134520 *
Number of reflections	22460
<I/σ(I)>	38.9
Completeness [%]	98.3	98.2
Redundancy	2.8	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	293	PEG 1000, PEG 8000, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12-37 (mg/ml)
2	1	reservoir	PEG1000	5-10 (%)
3	1	reservoir	PEG8000	5-10 (%)