1OLR

The Humicola grisea Cel12A Enzyme Structure at 1.2 A Resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-04-25
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	49.231, 49.231, 165.517
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.220 *
R-factor	0.13508
Rwork	0.135
R-free	0.15100 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h8v
RMSD bond length	0.013
RMSD bond angle	1.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.240
High resolution limit [Å]	1.220	1.220
Rmerge	0.076	0.352 *
Total number of observations	321815 *
Number of reflections	58847
<I/σ(I)>	24	4
Completeness [%]	94.6 *	84.4 *
Redundancy	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6	20-24 *	pH 6.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	cacodylate	0.02 (M)	pH6.0
2	1	reservoir	calcium acetate	0.02 (M)
3	1	reservoir	PEG2000 MME	10-30 (%(w/w))
4	1	drop	protein	20 (mg/ml)