1LP1

Protein Z in complex with an in vitro selected affibody

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	CCD
Collection date	2001-10-01
Detector	MARRESEARCH
Wavelength(s)	1.098
Spacegroup name	P 61 2 2
Unit cell lengths	55.546, 55.546, 155.749
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.225
Rwork	0.224
R-free	0.25500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Polyserine model of PDB entry 1DEE chain G
RMSD bond length	0.006
RMSD bond angle	1.170 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.050	0.290 *
Total number of observations	57198 *
Number of reflections	6847 *
Completeness [%]	99.7 *	99.8
Redundancy	8.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5 *	298	MgSO4, MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	72 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH7.5
3	1	reservoir		1.6 (M)
4	1	reservoir	MES	100 (mM)	pH6.5