Open AccessCrystallization and initial X‐ray diffraction studies of scaffolding protein (gp7) of bacteriophage ϕ29
Author(s) -
Anderson Dwight L.,
Badasso Mohammed O.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105008511
Subject(s) - orthorhombic crystal system , crystallography , crystallization , tetragonal crystal system , crystal (programming language) , crystal structure , solvent , molecule , molecular replacement , chemistry , materials science , organic chemistry , computer science , programming language
The Bacillus subtilis bacteriophage ϕ29 scaffolding protein (gp7) has been crystallized by the hanging‐drop vapour‐diffusion method at 293 K. Two new distinct crystal forms that both differed from a previously crystallized and solved scaffolding protein were grown under the same conditions. Form I belongs to the primitive tetragonal space group P 4 1 2 1 2, with unit‐cell parameters a = b = 77.13, c = 37.12 Å. Form II crystals exhibit an orthorhombic crystal form, with space group C 222 and unit‐cell parameters a = 107.50, b = 107. 80, c = 37.34 Å. Complete data sets have been collected to 1.78 and 1.80 Å for forms I and II, respectively, at 100 K using Cu K α X‐rays from a rotating‐anode generator. Calculation of a V M value of 2.46 Å 3 Da −1 for form I suggests the presence of one molecule in the asymmetric unit, corresponding to a solvent content of 50.90%, whereas form II has a V M of 4.80 Å 3 Da −1 with a solvent content of 48.76% and two molecules in the asymmetric unit. The structures of both crystal forms are being determined by the molecular‐replacement method using the coordinates of the published crystal structure of gp7.