1FN0

STRUCTURE OF A MUTANT WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN, N14D.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	1998-08-10
Detector	MARRESEARCH
Spacegroup name	P 61 2 2
Unit cell lengths	61.240, 61.240, 210.860
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.209 *
Rwork	0.209
R-free	0.28700
RMSD bond length	0.027 *
RMSD bond angle	2.100 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.000	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.087	0.423
Total number of observations	33037 *
Number of reflections	14503
<I/σ(I)>	3.5
Completeness [%]	75.7	68.8 *
Redundancy	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.4	4 *	Dattagupta, J.K., (1999) Proteins: Struct., Funct., Genet., 35, 321. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8.6 (mg/ml)
2	1	drop	Tris-HCl	71.4 (mM)
3	1	drop		286 (mM)
4	1	drop	ammonium sulfate	1.4 (%)
5	1	drop	sodium acetate	2.9 (mM)
6	1	reservoir	ammonium sulfate	25 (%)
7	1	reservoir	sodium acetate	60 (mM)