6NF3

Structure of the Monoclinic-3 (Monocln-3) Crystal Form of Human Apolipoprotein C1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-D
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1992-07-15
Detector	SDMS
Wavelength(s)	1.54
Spacegroup name	P 1 21 1
Unit cell lengths	38.169, 49.965, 35.423
Unit cell angles	90.00, 105.10, 90.00

Refinement procedure

Resolution	18.970 - 2.330
R-factor	0.20485
Rwork	0.199
R-free	0.31839
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rop
RMSD bond length	0.007
RMSD bond angle	1.093
Data reduction software	DENZO
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.500
High resolution limit [Å]	2.200	2.400
Rmerge	0.131	0.211
Rmeas	0.150	0.295
Rpim	0.071	0.206
Number of reflections	5846	263
<I/σ(I)>	4.6	1.7
Completeness [%]	70.0	46.2
Redundancy	2.6	1.2
CC(1/2)	0.987	0.933

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	298	The crystals were grown by sitting drop vapor diffusion in Cryschem plates using 0.6 ml reservoirs of 16% to 18% 2-methyl-2,4-pentanediol (MPD) containing o.1 M sodium acetate and 0.25% octyl-beta-s-1-thioglucopyanoside. The drops were equal volumes, generally 6 ul each, of the reservoir and an 8 mg/ml solution of protein dissolved in .02 M ammonium bicarbonate.