1FDP

PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	95
Detector technology	IMAGE PLATE
Collection date	1997-02-01
Detector	RIGAKU RAXIS IV
Spacegroup name	P 1 21 1
Unit cell lengths	65.050, 70.320, 86.300
Unit cell angles	90.00, 101.98, 90.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.204
Rwork	0.204
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CORE REGION OF FACTOR D (1DSU MOLECULE B)
RMSD bond length	0.008
RMSD bond angle	28.410 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.066	0.234
Total number of observations	93825 *
Number of reflections	43713
<I/σ(I)>	13.8	3.9
Completeness [%]	98.5	96.8
Redundancy	2.5	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7 *	298	CRYSTALLIZATION CONDITIONS: THE RESERVOIR SOLUTION CONTAINED 10-12% PEG-6000 AND 30MM MES (PH5.2). THE DROPS CONTAINED EQUAL VOLUME OF RESERVOIR SOLUTION AND PROTEIN SOLUTION (10MG/ML), VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)
3	1	drop		0.1 (M)
4	1	reservoir	PEG6000	10-12 (%)
5	1	reservoir	MES	30 (mM)