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A new member of class II chitinase from Phaseolus vulgaris was purified and crystallized. Diffraction data to 2.7Å resolution have been collected and the preliminary crystallographic studies have been completed. The space group is P1 with unit cell parameters of a=36.32Å, b=46.24Å, c=70.36Å, α =97.9 , β=103.8 and γ =110.5 . Molecular replacement and initial refinement statistics indicate there are two chitinase molecules in the crystallographic asymmetric unit.
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.