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Crystallization and preliminary X‐ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H‐D‐Phe‐Phe‐Arg‐chloromethylketone
Author(s) -
Banbula Agnieszka,
Potempa Jan,
Travis James,
Bode Wolfram,
Medrano FranciscoJavier
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070523
Subject(s) - porphyromonas gingivalis , orthorhombic crystal system , crystallography , crystallization , tetramer , chemistry , crystal structure , biology , bacteria , biochemistry , enzyme , genetics , organic chemistry
Gingipain R2 is a 50 kDa proteinase from the oral pathogenic bacterium Porphyromonas gingivalis . This proteinase, which displays no significant sequence homology to any protein previously analyzed by X‐ray crystallography, has been crystallized using the vapor diffusion method. Two different crystal forms were obtained from a solution containing polyethylene glycol (MW 8,000) (space group P2 1 2 1 2 1 ) or magnesium sulfate (space group R3) as precipitating agent. Complete diffraction data sets have been collected up to 2.0 and 2.9 Å resolution, respectively. Cell dimensions are a = 51.9 Å, b = 79.9 Å, and c = 99.6 Å (P2 1 2 1 2 1 ), and a = b = 176.6 Å, and c = 143.4 Å (R3). Considerations of the possible values of V m accounts for the presence of one monomer per asymmetric unit in the case of the orthorhombic crystal form, whereas the rhombohedral crystal form, together with the analysis of the self‐rotation function, could accommodate a tetramer in the asymmetric unit.