1NLR

ENDO-1,4-BETA-GLUCANASE CELB2, CELLULASE, NATIVE STRUCTURE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU FR-C
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1997-02-17
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 2
Unit cell lengths	48.492, 95.479, 40.519
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.750
R-factor	0.187 *
Rwork	0.187
R-free	0.24000
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	0.030
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.780
High resolution limit [Å]	1.750	1.750
Rmerge	0.047	0.287 *
Number of reflections	18747
<I/σ(I)>	31.4	5.96
Completeness [%]	93.7 *	67.9 *
Redundancy	6.77 *	2.78 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5		30 % PEG 1500, PH 4.5 FOR ACETATE BUFFER METHOD: HANGING DROP VAPOUR DIFFUSION, vapor diffusion

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	15 (mg/ml)
2	1	drop	acetate
3	1	reservoir	PEG1500	30 (%(w/w))