1OLQ

The Trichoderma reesei cel12a P201C mutant, structure at 1.7 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2000-12-03
Detector	MARRESEARCH
Spacegroup name	P 31
Unit cell lengths	70.616, 70.616, 69.092
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 1.700
R-factor	0.21035
Rwork	0.209
R-free	0.25100 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h8v
RMSD bond length	0.015
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.730
High resolution limit [Å]	1.700	1.700
Rmerge	0.074	0.390
Total number of observations	184371 *
Number of reflections	42832 *
<I/σ(I)>	18.3	2.8
Completeness [%]	99.8 *	99.6 *
Redundancy	4.3	99.6

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)