1BFF

THE 154 AMINO ACID FORM OF HUMAN BASIC FIBROBLAST GROWTH FACTOR

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1991-07
Detector	XUONG-HAMLIN MULTIWIRE
Spacegroup name	P 1
Unit cell lengths	30.800, 33.300, 36.500
Unit cell angles	64.10, 73.00, 76.10

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.19 *
Rwork	0.190
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	4fgf
RMSD bond length	0.020
RMSD bond angle	2.700
Data reduction software	XUONG-HAMLIN ((DETECTOR SYSTEM))
Data scaling software	XUONG-HAMLIN ((DETECTOR SYSTEM))
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.043 *
Total number of observations	15506 *
Number of reflections	7035
<I/σ(I)>	9.3	2.1
Completeness [%]	84.0	46
Redundancy	2.2	1.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5		THE PROTEIN WAS CRYSTALLIZED FROM 30-40 % PEG1000 AND 0.2-0.3 % 2-MERCAPTOETHANOL BY THE HANGING DROP VAPOR DIFFUSION METHOD., pH 7.5, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	hbFGF154		0.003-0.005ml
2	1	drop	PEG1000	15-20 (%)
3	1	drop	beta-mercaptoethanol	0.1-0.15 (%)
4	1	reservoir	PEG1000	30-40 (%)
5	1	reservoir	beta-mercaptoethanol	0.2-0.3 (%)