1AL8

THREE-DIMENSIONAL STRUCTURE OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS

Experimental procedure

Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1996-04
Detector	MARRESEARCH
Spacegroup name	I 4
Unit cell lengths	95.400, 95.400, 93.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.194
Rwork	0.194
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gox
RMSD bond length	0.007
RMSD bond angle	23.780 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.250
High resolution limit [Å]	2.200	2.200
Rmerge	0.094 *	0.369 *
Total number of observations	237398 *
Number of reflections	21308
<I/σ(I)>	7.9	3.3
Completeness [%]	99.8	99.9
Redundancy	11.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	8.3		PROTEIN WAS CRYSTALLIZED FROM 50MM TRIS- BUFFER, 0.25 MG/ML FMN, 4% TERTIARY BUTANOL AND 0.5 % JF 5969, PH 8.3. JF 5969 IS A MIXTURE OF SYMPERONIC NPE1800 (33.3G/L), TWEEN 85 (20G/L) IN CYCLOHEXANONE.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	20 (mg/ml)
2	1	1	Tris-HCl	0.05 (M)
3	1	1	GOX	0.5 (mg/ml)
4	1	1	FMN	0.25 (mg/ml)
5	1	1	JF5969	0.5 (%)
6	1	2	tertiary butanol	5 (%(v/v))