1FMZ

CRYSTAL STRUCTURE OF A MUTANT WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN, N14K.

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	1998-07-22
Detector	MARRESEARCH
Spacegroup name	P 61 2 2
Unit cell lengths	60.860, 60.860, 208.430
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.050
R-factor	0.193 *
Rwork	0.193
R-free	0.25300
RMSD bond length	0.012 *
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]	15.000	2.160
High resolution limit [Å]	2.050	2.050
Rmerge	0.082	0.282
Total number of observations	147330 *
Number of reflections	13051
<I/σ(I)>	5.2
Completeness [%]	88.1	91.8 *
Redundancy	4.3	5.4

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)