1KCM

Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution

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	1999-12-09
Detector	ADSC QUANTUM 4r
Wavelength(s)	0.9322
Spacegroup name	P 32 2 1
Unit cell lengths	50.464, 50.464, 216.105
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.000
R-factor	0.216 *
Rwork	0.216
R-free	0.27300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1FVZ
RMSD bond length	0.012
RMSD bond angle	1.420 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.060
High resolution limit [Å]	1.990	1.990
Rmerge	0.051	0.171
Total number of observations	231585 *
Number of reflections	22060	2012 *
<I/σ(I)>	25.7	7.3
Completeness [%]	96.7	91.1
Redundancy	4.33 *	2.70 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2 *	4 *	11% PEG 6000, 0.2M calcium acetate, 100MM cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)	pH7.2
3	1	drop	beta-mercaptoethanol	10 (mM)
4	1	reservoir	PEG6000	11 (%(w/v))
5	1	reservoir	calcium acetate	200 (mM)
6	1	reservoir	cacodylate	100 (mM)	pH6.5