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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Expression, purification and preliminary X-ray characterization of N-acetyl-gamma-glutamyl-phosphate reductase from Thermus thermophilus HB8.

N-Acetyl-gamma-glutamyl-phosphate reductase (AGPR) catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate to give the N-acetylglutamic semialdehyde. A recombinant form of AGPR from Thermus thermophilus HB8 has been crystallized by the hanging-drop vapour-diffusion technique using PEG 4000 as a precipitating agent. The crystals grew as colourless prisms, with unit-cell parameters a = b = 90.9, c = 139.5 A, alpha = beta = 90, gamma = 120 degrees. The crystals belong to the hexagonal space group P6(2)22 or P6(4)22 and are most likely to contain a monomer in the asymmetric unit, with a V(M) value of 2.19 A(3) Da(-1). The crystals diffract to a resolution of 2.2 A at beamline BL44B2 of SPring-8.[1]

References

  1. Expression, purification and preliminary X-ray characterization of N-acetyl-gamma-glutamyl-phosphate reductase from Thermus thermophilus HB8. Goto, M., Agari, Y., Omi, R., Miyahara, I., Hirotsu, K. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
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