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Expression, purification, crystallization and preliminary crystallographic study of FtsA from methicillin-resistant Staphylococcus aureus.

ABSTRACT: FtsA from methicillin-resistant Staphylococcus aureus (MRSA) was cloned, overexpressed and purified. The protein was crystallized using the sitting-drop vapour-diffusion technique. A cocrystal with ?-?-imidoadenosine 5'-phosphate (AMPPNP; a nonhydrolysable ATP analogue) was grown using PEG 3350 as a precipitant at 293 K. X-ray diffraction data were collected to a resolution of 2.3 Å at 100 K. The crystal belonged to the monoclinic space group P2?, with unit-cell parameters a = 75.31, b = 102.78, c = 105.90 Å, ? = 96.54°. The calculated Matthews coefficient suggested that the asymmetric unit contained three or four monomers.

SUBMITTER: Fujita J 

PROVIDER: S-EPMC3729168 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary crystallographic study of FtsA from methicillin-resistant Staphylococcus aureus.

Fujita Junso J   Miyazaki Yuma Y   Hirose Mika M   Nagao Chioko C   Mizohata Eiichi E   Matsumoto Yoshimi Y   Mizuguchi Kenji K   Inoue Tsuyoshi T   Matsumura Hiroyoshi H  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130727 Pt 8

FtsA from methicillin-resistant Staphylococcus aureus (MRSA) was cloned, overexpressed and purified. The protein was crystallized using the sitting-drop vapour-diffusion technique. A cocrystal with β-γ-imidoadenosine 5'-phosphate (AMPPNP; a nonhydrolysable ATP analogue) was grown using PEG 3350 as a precipitant at 293 K. X-ray diffraction data were collected to a resolution of 2.3 Å at 100 K. The crystal belonged to the monoclinic space group P2₁, with unit-cell parameters a = 75.31, b = 102.78,  ...[more]

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