2D26

Active site distortion is sufficient for proteinase inhibit second crystal structure of covalent serpin-proteinase complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2004-12-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	109.830, 85.180, 76.260
Unit cell angles	90.00, 121.01, 90.00

Refinement procedure

Resolution	50.000 - 3.300
R-factor	0.256
Rwork	0.251
R-free	0.31200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ezx 1h9l
RMSD bond length	0.010
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.450
High resolution limit [Å]	3.300	3.300
Rmerge	0.078	0.275
Number of reflections	8959
<I/σ(I)>	9.5	5.7
Completeness [%]	97.8	96.4
Redundancy	3.6	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.1	291	PEG3350, pH 8.10, VAPOR DIFFUSION, HANGING DROP, temperature 291K