1LU0

Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	100
Detector technology	CCD
Collection date	2000-04-07
Detector	MARRESEARCH
Wavelength(s)	0.8919
Spacegroup name	P 21 21 2
Unit cell lengths	47.280, 58.630, 19.320
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.030
R-factor	0.1206
Rwork	0.120
R-free	0.13950 *
Structure solution method	Dual-space recycling
RMSD bond length	0.025
RMSD bond angle	2.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXD
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.070
High resolution limit [Å]	1.030	1.030
Rmerge	0.047	0.151
Total number of observations	252201 *
Number of reflections	27045
<I/σ(I)>	30.7	2.73
Completeness [%]	99.2	98.3
Redundancy	9.3	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	PEG 8000, zinc sulfate, cacodylate, MPD, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		5 (mM)
2	1	reservoir	cacodylate	50 (mM)	pH6.5
3	1	reservoir	MPD	14 (%)
4	1	reservoir	PEG8000	8 (%)
5	1	drop	protein	12 (mg/ml)