Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 2 (February 2008)

crystallization communications

Acta Cryst. (2008). F64, 91-93 [ doi:10.1107/S1744309107068649 ]

Purification, crystallization and preliminary crystallographic analysis of the non-Pfam protein AF1514 from Archeoglobus fulgidus DSM 4304

P. Bahti, S. Chen, Y. Li, N. Shaw, X. Zhang, M. Zhang, C. Cheng, G. Song, J. Yin, H. Zhang, D. Che, A. Abbas, H. Xu, B.-C. Wang and Z.-J. Liu

Abstract: A 10.5 kDa non-Pfam hypothetical protein, AF1514, from the hyperthermophilic archaeon Archeoglobus fulgidus has been overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted X-rays to 2.09 Å resolution and a data set was collected at 100 K using Cu K [alpha] radiation from a rotating-anode X-ray source. The crystals belong to space group P4₁2₁2 or P4₃2₁2, with unit-cell parameters a = b = 49.27, c = 106.61 Å. The calculated Matthews coefficient was 3.16 Å³ Da^-1, suggesting the presence of one molecule in the asymmetric unit.

Keywords: non-Pfam proteins; reductive methylation.