Solvent content of protein crystals

Matthews, Brian W.

doi:10.1016/0022-2836(68)90205-2

Cited by 8,050 publications

(4,878 citation statements)

References 32 publications

Supporting

203

Mentioning

4,638

Contrasting

Unclassified

Order By: Relevance

“…Assuming four Fab molecules (of M, 50,000 each) per asymmetric unit, the specific volume of the protein is 3.02 A3/Da, which is within the range normally observed for protein crystals (Matthews, 1968) and corresponds to a 59% (v/v) solvent content. Attempts to determine the structure by a molecular replacement method using existing Fab structures as search models are in progress.…”

Section: Crystallization Of Fab Fragment Of Pathogenic Rat Mab Againsmentioning

confidence: 62%

Crystallization and preliminary crystallographic study of an Fab fragment of a pathogenic rat monoclonal antibody against the nicotinic acetylcholine receptor

et al. 1993

View full text Add to dashboard Cite

Section: Crystallization Of Fab Fragment Of Pathogenic Rat Mab Againsmentioning

confidence: 62%

Crystallization and preliminary crystallographic study of an Fab fragment of a pathogenic rat monoclonal antibody against the nicotinic acetylcholine receptor

et al. 1993

View full text Add to dashboard Cite

“…The final structure was refined to 2.5 Å resolution with a final R work value of 23.1% (R free = 26.7%). The crystal belongs to the space group P4 1 2 1 2, and there is one molecule in an asymmetric unit with a Matthews coefficient of 2.6 Å 3 /Da (corresponding to 43% solvent content) (Matthews, 1968).…”

Section: Monomer Folding Of Snac1 Nac Domainmentioning

confidence: 99%

A structural view of the conserved domain of rice stress-responsive NAC1

et al. 2011

View full text Add to dashboard Cite

The importance of NAC (named as NAM, ATAF1, 2, and CUC2) proteins in plant development, transcription regulation and regulatory pathways involving proteinprotein interactions has been increasingly recognized. We report here the high resolution crystal structure of SNAC1 (stress-responsive NAC) NAC domain at 2.5 Å. Although the structure of the SNAC1 NAC domain shares a structural similarity with the reported structure of the ANAC NAC1 domain, some key features, especially relating to two loop regions which potentially take the responsibility for DNA-binding, distinguish the SNAC1 NAC domain from other reported NAC structures. Moreover, the dimerization of the SNAC1 NAC domain is demonstrated by both soluble and crystalline conditions, suggesting this dimeric state should be conserved in this type of NAC family. Additionally, we discuss the possible NAC-DNA binding model according to the structure and reported biological evidences.

show abstract

“…The volume to mass ratio is V,,, = 2.20 A3/dalton which is near the center of the range found for most protein molecules (Matthews, 1968). The asymmetric unit of the crystals must, therefore, be composed of a single lipase molecule.…”

mentioning

confidence: 76%

Preliminary investigation of crystals of the neutral lipase from Pseudomonas fluorescens

Larson

Day

Greenwood

et al. 1991

Journal of Molecular Biology

View full text Add to dashboard Cite

The neutral lipase from the bacteria Pseudomonas jluorescens, marketed under the trade name LpL-BOOS, has been crystallized in a form suitable for X-ray diffraction analysis from 35% n-propanol at pH 8.5. The crystals are monoclinic prisms and are of space group C2 with a = 9160 A, b = 47.17 A, c = 35.21 A and /Y? = 121.43". There is one molecule of the protein as the asymmetric unit of the crystals. The diffraction pattern extends to at least 1.6 A resolution and the crystals are extremely robust in terms of X-ray exposure.

show abstract

Solvent content of protein crystals

Cited by 8,050 publications

References 32 publications

Crystallization and preliminary crystallographic study of an Fab fragment of a pathogenic rat monoclonal antibody against the nicotinic acetylcholine receptor

Crystallization and preliminary crystallographic study of an Fab fragment of a pathogenic rat monoclonal antibody against the nicotinic acetylcholine receptor

A structural view of the conserved domain of rice stress-responsive NAC1

Preliminary investigation of crystals of the neutral lipase from Pseudomonas fluorescens

Contact Info

Product

Resources

About