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Crystallization and preliminary X‐ray diffraction data of two heparin‐binding fragments of human fibronectin
Author(s) -
Pechik Lgor,
Nachman Joseph,
Ingham Kenneth,
Gilliland Gary L.
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340160105
Subject(s) - orthorhombic crystal system , ammonium sulfate , crystallization , polyethylene glycol , crystallography , chemistry , crystal (programming language) , crystal structure , molecule , materials science , chromatography , organic chemistry , computer science , programming language
Two different heparin‐binding fragments of human fibronectin have been crystallized in forms which are suitable for crystal structure analyses. The 30 kDa hep‐2A fragment, consisting of type III domains 12–14, was crystallized from solutions containing ammonium sulfate or polyethylene glycol 6000. The crystals grown in ammonium sulfate solutions were orthorhombic with space group I 222 or I 2 1 2 1 2 1 with a = 68.1 Å, b = 88.6 Å, and c = 144.9 Å. The crystals grown in polyethylene glycol solutions are hexagonal with space group P 6 1 22 or P 6 5 22 witha a = b = 66.7 Å and c = 245.7 Å. The 40 kDa hep‐2B fragment, consisting of type III domains 12–15, was also crystallized from solutions containing ammonium sulfate with the addition of glycerol. Glycerol proved an effective agent for reducing the number of crystals in the crystallization experiments, and thus, increasing the size of the crystals in these experiments. This crystal form is nearly isomorphous to the orthorhombic form of the hep‐2A fragment with space group I 222 or I 2 1 2 1 2 1 and a = 67.5 Å, b = 87.0 Å, and c = 144.3 Å. All crystal forms diffract to at least 3.5 Å resolution and contain a single molecule in the asymmetric unit. © 1993 Wiley‐Liss, Inc.